Publication for Anxa2 and S100a10

Species Symbol Function* Entrez Gene ID* Other ID Gene
coexpression		 CoexViewer
mmu Anxa2 annexin A2 12306 [link]
mmu S100a10 S100 calcium binding protein A10 (calpactin) 20194

Pubmed ID Priority Text
24002251 0.99 p11 and annexin A2 shuttle between cytoplasm and nucleus, and that the nuclear export signal (NES) located in the N-terminus of annexin A2 (Fig 3B) plays a critical role in the nuclear export of p11 as well as annexin A2.
0.98 P11 can be targeted to membranes via complex formation with annexin A2 probably in a Ca2+-regulated manner because the annexin A2 subunit requires Ca2+ for efficient membrane binding.
0.98 p11 and annexin A2 are up-regulated in hippocampus after chronic SSRI administration in wild-type mice (Fig 4).
0.98 p11/annexin A2, SMARCA3 promotes its own localization to the nuclear matrix fraction, the subnuclear region where critical nuclear events, such as gene expression, replication and repair processing, occur.
0.98 p11/annexin A2 also increases its DNA-binding affinity and transcriptional activity.
0.98 p11/annexin A2/SMARCA3 complex remodels chromatin and regulates gene transcription.
0.97 p11 was initially identified within a heterotetrameric complex that it forms with annexin A2.
0.97 annexin A2 that form an amphiphatic alpha-helix are sufficient for p11 binding (Fig 3B).
0.97 p11/annexin A2 heterotetramer.
0.97 p11 and annexin A2 induction facilitates the assembly of the p11/annexin A2/SMARCA3 complex.
0.97 p11/annexin A2/SMARCA3 complex contributes to multiple stages of antidepressant-stimulated neurogenesis.
0.97 p11 and annexin A2 mRNA and protein levels are up-regulated in hippocampus and cortex after chronic SSRI administration, and this upregulation is likely to be mediated by 5-HT receptors.
0.96 p11 participate in annexin A2 binding.
0.96 p11/annexin A2 in complex with the motif peptides found in SMARCA3 or AHNAK1 revealed that p11 and annexin A2 cooperate to create a unique binding pocket for SMARCA3 or AHNAK1 motif peptide (Fig 3G for the complex with SMARCA3 peptide).
0.96 p11/annexin A2/SMARCA3 complex appears, thus, to be an important mediator of antidepressant responses.
0.96 p11 participate in annexin A2 binding.
0.94 p11/annexin A2 increases after antidepressant administration.
0.93 p11 in complex with the N-terminal region from annexin A2 showed that the four helices from each monomer are arranged in an antiparallel manner, and that the p11 dimer contains two identical annexin A2-binding sites (a hydrophobic cleft formed by the C-terminal region from one monomer and the Helix I from the other monomer), forming a heterotetramer (Fig 3C).
0.92 p11 (also known as S100A10, nerve growthfactor-induced protein 42C, calpactin I light chain, and annexin II light chain).
0.92 p11/annexin A2/SMARCA3.
0.92 p11/annexin A2/SMARCA3 chromatin remodeling complex and to determine which of these are involved in mediating therapeutic responses to antidepressants.
0.92 p11/annexin A2 complex binds to 2 molecules of SMARCA3 and the heterohexameric complex is then targeted to the nuclear matrix.
0.87 p11 and annexin A2 may reveal valuable and novel therapeutic targets.
0.86 p11, annexinA2 and SMARCA3
0.71 p11 binding motif in 5-HTRs and the role of annexin A2 in the interaction between p11 and 5-HTRs remain to be studied.
0.69 P11/annexin A2 binding motif is located in the N-terminus (aa 34-39).
0.67 Annexin A2 is composed of p11 binding motif (aa 2-12) and NES motif in the N-terminus, and four annexin repeat domains, each of which is 70 amino acids long and composed of five alpha-helices.
0.64 p11 and annexin A2, the levels of SMARCA3 protein and mRNA were not altered after treatment with SSRI.
0.58 p11 forms a heterotetramer with annexin A2.
26370144 0.99 p11/annexin A2 complex binds to a chromatin-remodeling factor named SMARCA3 to regulate gene transcription.
0.98 p11, indicating that AnxA2 is required for the interaction of p11 with mGluR5 (Figure 1a).
0.97 p11 and annexin A2 are elevated in the cortex and hippocampus.
0.96 p11-AnxA2 fusion protein (Figures 1c and d).
0.95 p11/annexin A2 heterotetramer provides two hydrophobic pockets for the binding of a conserved binding motif, which is represented by phi-P-#-F-X-F (phi: hydrophobic amino acid, P: proline, #: basic amino acid, F: phenylalanine, X: any amino acid) and is located in the N-terminus of SMARCA3.
0.89 p11 and annexin A2 is upregulated by other mechanisms such as phosphorylation.
0.77 p11 fused to an N-terminal peptide of AnxA2 (GST-p11-AnxA2 fusion protein) which mimics p11/AnxA2 heterotetramers (Figure 1b).
23415230 0.98 p11/annexin A2 heterotetrameric complex.
0.98 p11 is induced in both cell types, and the amount of the ternary complex of p11/annexin A2/SMARCA3 is increased.
0.98 AnxA2 together with p11 plays a role in trafficking of membranous/cytoplasmic proteins to plasma membrane or in providing them with firm anchorage at the plasma membrane and the cytoskeletal structure.
0.98 p11/AnxA2 complex.
0.98 AnxA2 is drastically down-regulated in the frontal cortex and hippocampus of p11 KO mice (Figure 1A), in spite of unchanged levels of AnxA2 transcript (Figure 1B).
0.98 p11 KO mice, indicating the specificity of the physiological interaction between p11 and AnxA2 in the brain (Figure 1A).
0.98 p11 significantly decreased the interaction with AnxA2, without altering the interaction with endogenous p11 to form a p11 dimer, suggesting that C83 mutations selectively interfere with the heterotetramer formation, but not the homodimerization of p11 molecules (Figure S1A).
0.98 p11/AnxA2 interaction, is not (Figure 4D), confirming the importance of the p11/AnxA2 complex in the subnuclear localization of SMARCA3.
0.98 p11/AnxA2 not only increases the DNA binding affinity of SMARCA3, but also anchors SMARCA3 to the nuclear matrix presumably via the interaction of AnxA2 with actin and PIP2.
0.98 p11/AnxA2 regulates transcriptional activity of SMARCA3 by controlling the DNA binding affinity of SMARCA3, as well as its localization.
0.98 AnxA2 together with p11 is induced by fluoxetine and requires p11 for its protein stability (Figure 1D and 1E).
0.98 p11/AnxA2 facilitates the DNA binding affinity of SMARCA3 (Figure 4A and 4B).
0.98 p11/AnxA2, may lead to the activation of SMARCA3 to initiate ATP-dependent chromatin remodeling of the target genes.
0.98 p11/AnxA2 binding to SMARCA3 would open the chromatin structure and recruit specific transcription factors bound to the C-terminal domain of SMARCA3 to the specific locus of the genomic DNA.
0.98 p11/AnxA2 mediates the subnuclear targeting of SMARCA3 (Figure 4C and 4D).
0.98 p11/AnxA2 to localize properly to the distinct subcellular sites where they become functionally active.
0.97 p11 and AnxA2 were also found to localize in the nucleus and interact with nuclear proteins, although the precise roles of p11 and AnxA2 in the nucleus have not been clearly defined.
0.97 p11, together with AnxA2, form a heterotetramer in cells.
0.97 p11 and AnxA2 exist as a protein complex, which can be induced by antidepressant administration.
0.97 p11/AnxA2.
0.97 p11/AnxA2 binds to PIP2 as well as actin.
0.97 p11 together with AnxA2 shuttles between cytoplasm and nucleus (data not shown).
0.97 p11 and AnxA2 induction facilitates the assembly of the p11/AnxA2/SMARCA3 complex.
0.97 p11/AnxA2/SMARCA3 complex-mediated hippocampal neurogenesis may contribute to the behavioral response to SSRIs.
0.96 p11/AnxA2/SMARCA3 pathway mediates both neurogenic and behavioral responses to SSRIs.
0.96 p11 exists in a protein complex with AnxA2 in brain tissue.
0.96 p11 and AnxA2 in the brain.
0.96 p11/AnxA2.
0.96 p11-AnxA2 peptide cassette is mediated by van der Waals contacts and hydrogen bond interactions, whereby the SMARCA3 peptide interacts with elements of both p11 and AnxA2 peptide (Figure 3D).
0.96 p11/AnxA2/SMARCA3 by about 2.3 fold (Figure 6F).
0.96 p11/full length AnxA2/SMARCA3 peptide visualized the spatial organization of each component in the ternary complex, in which the p11 dimer is ideally positioned in the core of the complex to link SMARCA3 to AnxA2 (Figure 3G).
0.96 p11/AnxA2/SMARCA3 signalling pathway is non-cell autonomous.
0.95 p11/AnxA2 (Figure S3A).
0.95 AnxA2 abolished the interaction with SMARCA3 with no effect on p11 interaction, whereas Leu8A and Leu11A mutation blunted the interaction to p11 as well as to SMARCA3 (Figure S3B), showing a unique role of the Leu13 residue in creating a binding pocket for the ternary targets.
0.95 p11/AnxA2 interaction may regulate the DNA-binding affinity of SMARCA3.
0.95 p11/AnxA2 and the B-box oligonucleotide (Figure 4A).
0.95 p11/AnxA2 may regulate the subnuclear localization of SMARCA3.
0.95 p11/AnxA2/SMARCA3 complex is increased after treatment with FLX for 2 weeks.
0.94 p11/AnxA2 complex.
0.94 p11(170.4+-7.3% of p11(+/+)-VEH group, p=0.004) and of AnxA2 (167.1+-20.8%, p=0.042) (Figure 1D and 1E).
0.94 p11/full-length AnxA2/SMARCA3 peptide illuminated the three dimensional organization of each component within the ternary complex (Figure 3G).
0.93 Annexin A2 (AnxA2) is a well characterized binding partner for p11.
0.93 p11/AnxA2.
0.92 p11 and the interaction was greatly reduced or abolished by either C83S or C83Q mutation of p11, indicating that the interaction likely needs AnxA2 binding to p11.
0.91 p11 alone and the p11-AnxA2 peptide cassette are disrupted due to the movement of the Asp58-Asp64 loop on complex formation.
0.91 p11/AnxA2/SMARCA3 Complex in Hilar Mossy Cells and Basket Cells in the Dentate Gyrus
0.91 p11/AnxA2/SMARCA3 complex.
0.91 p11 and AnxA2 act as regulatory proteins but are not likely structural core components of SMARCA3.
0.91 p11/AnxA2 in mediating the membrane translocation of AHNAK1.
0.90 p11 and AnxA2 cooperate to create a unique binding pocket, but the optimal binding condition is not achieved without conformational changes associated with target binding.
0.89 p11/AnxA2 Complex
0.89 p11/AnxA2/SMARCA3 pathway should contribute not only to our understanding of SSRI actions, but also provide molecular and cellular targets for the development of advanced therapeutics for mood and anxiety disorders.
0.88 p11/AnxA2 Complex
0.88 p11 Asp60 residue abolished the interaction with SMARCA3 while maintaining homodimerization of p11, as well as heterotetramer formation with AnxA2, although the D60A mutant of p11 displayed a decrease in protein stability (Figure S3C).
0.88 AnxA2 is composed of an N-terminal p11 binding region and a C-terminal annexin repeat region with opposing convex and concave sides.
0.88 p11 and AnxA2 potentiated luciferase activity (Figure 4E).
0.87 p11 protein level in the hippocampal lysates from AnxA2 knockout mice is reduced (data not shown).
0.87 p11/AnxA2 (Figure 2F; data not shown for AHNAK2 peptide).
0.87 p11/AnxA2 as an Antidepressant-Regulated Protein Complex
0.86 p11/AnxA2 Complex
0.84 p11 protein requires AnxA2 for its protein stability (data not shown).
0.81 p11 and AnxA2 stabilize each other as structural components of a protein complex (Figure 1), the levels of p11 and AnxA2 are not altered in SMARCA3 KO mice (Figure S5B and S5C) and the level of SMARCA3 is not altered in p11 KO mice (data not shown).
0.78 p11/AnxA2 interaction increases the DNA binding affinity of SMARCA3 by up to 2.5 fold, whereas the equivalent amount of AnxA2 alone didn't show any effect (Figure 4B).
0.77 AnxA2 contact the lateral/bottom side of the inverted p11 homodimer, two N-terminal peptides of SMARCA3 are anchored on the top position of the inverted p11 dimer while crossing each other.
0.75 p11/AnxA2/SMARCA3 Complex in Antidepressant Action
0.75 p11/AnxA2 Complex
0.68 p11 (Phe42, Ile55, Leu59, Leu75, Leu79, Ala82) and AnxA2 peptide (Leu8, Leu11, Leu13) in the complex (Figure 3E), with similar interactions observed for Pro5664 and Phe5666 in the AHNAK1 complex (Figure S2E).
0.66 p11 and SMARCA3 in the excitability and synaptic transmission of basket cells and mossy cells?; which genes are regulated by the p11/AnxA2/SMARCA3 complex in basket cells and mossy cells?; which of these genes contribute to the neurogenic and behavioral responses to antidepressants?
0.62 p11 and Ser12 in AnxA2 flip inward toward the peptide-binding groove, forming additional intermolecular hydrogen bonds (Figure 3D-3F).
0.61 p11/AnxA2 with SMARCA3
0.60 p11 and AnxA2 (Figure 1D and 1E), the levels of SMARCA3 protein (Figure 6D) and mRNA (Figure 6E) were not altered after treatment with fluoxetine.
0.57 p11/AnxA2 heterotetramer has additional binding pocket(s) on the surface.
30760886 0.98 p11/Anxa2 protein complex and a pivotal regulator of L-type VGCCs in the brain.
0.98 p11 in various tissues from Anxa2 knockout (KO) mice.
0.98 Anxa2 caused p11 degradation in a proteasome-dependent manner, suggesting a role for Anxa2 interaction in the stabilization of p1146.
0.98 Anxa2 was also drastically reduced without alteration of its mRNA level in brains of p11 KO mice, supporting the physiological relevance of the interaction between the components of the p11/Anxa2 protein complex.
0.98 p11 and Anxa2 are required for the surface recruitment of Ahnak to the cell membrane.
0.98 p11/Anxa2 protein complex, stabilizes p11 and Anxa2 proteins in the brain.
0.97 p11 and Anxa2 proteins in the hippocampus and prefrontal cortex in rodent brain.
0.97 p11 forms a heterotetrameric protein complex with Anxa2.
0.97 p11/Anxa2 complex in the brain.
0.97 p11/Anxa2 protein complex stabilize each other in cells.
0.97 p11 and Anxa2 were drastically reduced in the hippocampus (Figure 1d and e) and prefrontal cortex (PFC) (Figure 1f and g) of Ahnak KO mice compared to their wild-type (WT) controls.
0.97 p11 and Anxa2 in the hippocampus (Figure 1h and i) and PFC (Figure 1j and 1k) are highly and positively correlated.
0.97 p11/Anxa2 hybrid-immobilized beads but not by GST-immobilized beads (Figure 3a), suggesting that L-type VGCCs interact with the Ahnak/p11/Anxa2 complex.
0.97 p11/Anxa2 complex.
0.97 p11/Anxa2 complex, stabilizes p11 and Anxa2 proteins.
0.96 p11 and Anxa2 are highly and positively correlated in the brain.
0.96 p11/Anxa2 complex, revealing a novel molecular connection involved in the control of depressive behavior.
0.96 p11 and Anxa2 proteins in primary cultured cortical neurons derived from Ahnak KO embryos (Supplementary Figure 1c).
0.96 p11/Anxa2 complex as an endogenous neuronal machinery controlling cell surface expression of L-type VGCCs and thereby scaling neuronal activity-induced calcium signaling.
0.95 p11/Anxa2 complex, stabilizes p11 and Anxa2 proteins in the brain
0.95 p11 and Anxa2 (Figure 1c).
0.95 p11 and Anxa2 proteins and positive correlation in the levels of Ahnak, p11 and Anxa2 support the existence of the Ahnak/p11/Anxa2 complex in the brain.
0.95 p11 and Anxa2 are positively correlated in an individual brain tissue (n=29).
0.93 p11 and Anxa2 (Figure 3c), which is consistent with previous reports for the interaction of the C-terminal region of Ahnak with p11/Anxa212 and beta2 subunit.
0.92 p11/Anxa2 hybrid mimics the property of the heterotetrameric holocomplex in formation of a hydrophobic pocket for the binding to its effector proteins such as SMARCA3 and Ahnak.
0.92 p11/Anxa2 through its C-terminal region.
0.88 p11/Anxa2 complex and L-type voltage-gated calcium channel and modulates depressive behavior
0.88 p11/Anxa2 complex in the brain.
0.87 p11/Anxa2 complex.
0.86 p11/Anxa2 complex.
0.86 p11/Anxa2 complex in the brain.
0.81 p11/Anxa2 complex was characterized in cell line, yeast triple-hybrid assays and in vitro experiments.
0.80 p11/Anxa2 protein complex.
0.72 p11/Anxa2 complex, did not alter protein levels of p11 and Anxa29.
0.68 p11/Anxa2 complex in the brain has not yet been investigated.
0.54 p11 and Anxa2 proteins and in regulating L-type VGCCs, we examined whether the loss of Ahnak results in depression-like or antidepressant-like behaviors by measuring depression-related behaviors.
0.51 p11/Anxa2 complex at atomic level.
22505935 0.98 AnxA2 is mostly found in a stable heterotetramer with S100A10, a small, EF-hand protein that is unique within its own family in being able to bind calcium.
0.98 AnxA2/S100A10 complex formation) across a calcium switch experiment blocked tight junction reformation, consistent with the idea that extracellular AnxA2 plays an important role in remodeling of tight junctions.
0.97 S100A10 and two AnxA2 molecules, has a higher affinity for calcium and phospholipid than the AnxA2 monomer alone and is found associated with the cytoplasmic leaflet of the plasma membrane and specific membrane-bound structures, such as endosomes and transport intermediates.
0.97 AnxA2-S100A10 complex to these membrane sites, although it often remains associated with these membrane domains after the initial calcium pulse has subsided (our unpublished observations).
0.97 AnxA2 monomer alone (without associated S100A10) is able to "cap" the fast-growing "barbed" end of the growing actin filament and possibly also interacts directly with G-actin monomers.
0.97 AnxA2 is expressed at particularly high levels in epithelia and endothelia intracellularly, but it also appears as an extracellular, cell-surface-associated pool in complex with S100A10.
0.96 AnxA2 and the AnxA2-S100A10 tetrameric complex to bind and bundle filamentous actin (F-actin) was first identified using proteins purified from the brush-borders of porcine epithelial cells and from A431 cells.
0.93 S100A10, indicating that the cholesterol-dependent association of AnxA2 with endosomes does not require formation of the tetrameric complex.
0.91 AnxA2/S100A10 fusion protein is introduced into cells (which causes aggregation of AnxA2), early endosomes are also aggregated.
0.81 AnxA2 mouse is also effectively an S100A10 knockout animal as AnxA2 serves to prevent S100A10 degradation in the cytoplasm.
0.61 AnxA2/S100A10 fusion protein was introduced into the cells (which caused the aggregation of AnxA2), early endosomes were also aggregated.
0.60 AnxA2 (as is seen in some cancers) or nonstoichiometric changes in the relative concentrations of AnxA2 and S100A10 may have more severe phenotypes than loss of both.
10459018 0.98 annexin II-p11 heterotetramer with the plasma membrane, but not with the submembranous cytoskeleton, induces the tyrosine phosphorylation of annexin II, presumably exposing the tyrosine-phosphorylation site as a consequence of induced conformational changes (Bellagamba et al. 1997).
0.97 annexin II-p11 aggregates caused by expression of a trans-dominant mutant of annexin II resulted in coclustering of CD44.
0.97 annexin II exists as a heterotetramer bound to its ligand p11.
0.97 annexin II might interact with the submembranous actin network with this activity depending on its ability to form the heterotetrameric annexin II-p11 complex and on the presence of intact Ca2+-binding sites (Thiel et al. 1992).
0.97 annexin II-p11 chimera, acting as a trans-dominant mutant, causes aggregation of annexin II-p11 tetramers.
0.96 annexin II occurs either as a 36-kD monomer (p36) or as a heterotetrameric complex (p90) coupled with the S-100-related protein, p11 (Kube et al. 1992; Harder and Gerke 1994).
0.95 annexin II-p11 aggregates did not affect the actin-based cell cortex, but translocated early endosomes (Harder and Gerke 1993).
0.94 p11 dimers bound to this chimera would accommodate additional sites for binding of chimera and/or annexin II-p11 complexes, leading to the formation of the large aggregates containing annexin II, p11, and the chimeric protein.
0.94 annexin II-p11-positive clusters underneath the plasma membrane was observed (Fig. 4 A).
0.87 annexin II- p11 tetramer is significantly enriched in the Triton X-100-insoluble fraction of MDCK cells in the presence of Ca2+ (Harder and Gerke 1994).
22453828 0.98 annexin A2 and S100A10 are readily recruited to the endosomal membrane following organelle destabilization.
0.98 annexin A2-S100A10)2 is sufficient to aggregate membranes.
0.98 annexin A2-S100A10-mediated membrane aggregation.
0.98 annexin A2 and S100A10 are recruited to the endosomal membrane as an attempt to restore membrane integrity.
0.97 annexin A2-mediated membrane bridging, it has been postulated that, in the presence of Ca2+ and at pH 7.4, the conserved Ca2+-binding domains, within the core domain of an annexin A2 dimer, mediate electrostatic interactions with PS located in the membrane to be fused, whereas the Ca2+-binding S100A10 stabilizes the annexin A2 dimer, thus bridging the gap between the two membranes (Fig. 7c).
0.97 annexin A2 endosomal binding is also associated with increased S100A10 recruitment.
0.96 annexin A2-S100A10)2 complex recruits cytosolic vesicles to bridge micrometre size gaps.
0.93 annexin A2-S100A10)2 complex bridges submicrometre membrane gaps.
28179399 0.98 S100a10, a membrane protein that forms a hetero-tetrameric complex with annexin A2.
0.98 S100a10 and annexin A2 are also enriched by 19.9-fold and 7.7-fold, respectively, in the liver proteome of the fatty liver, correlating with significant accumulation of annexin A2/S100a10 complex in LD sub-organelles of the fatty liver (Fig. 4C, Fig. 5A).
0.98 S100a10 and its binding partner, annexin A2, were enriched in liver LDs in physiological conditions, and were further increased with HFD.
0.97 annexin A2/S100a10 complex has been reported as being upregulated in many cancers, including HCC.
0.96 S100a10, a component of annexin A2 heterotetramer complex, accelerated hepatosteatosis induced by HFD.
19520970 0.98 annexin 2, alpha-enolase, H2B and p11, increased by 3-4 fold (Figure 1B, first panel & C) as measured by Western blots with specific antibodies to each protein.
0.97 annexin 2 and p11 on the surface (cells were not permeabilized) of arrested macrophages (Figure 7A) in Plg-/- mice.
0.94 annexin 2 and p11, all proteins which lack signal sequences for cell-surface export.
0.92 annexin 2 and p11.
22848640 0.98 AnxA2 is part of a heterotetramer complex comprising two AnxA2 monomers and two copies of its natural binding partner, p11.
0.98 AnxA2 is translocated to the cell surface through a p11-dependent mechanism and is found at the cell surface of epithelial and endothelial cells.
0.95 AnxA2 is composed of an N-terminal 23 aa segment that binds p11, followed by four repeat structures (R1-R4).
0.95 AnxA2 in all hepatocytes may be needed to lower LDLc levels, or the co-expression of its p11 partner, expressed at very low levels in the liver, may be required for more effective translocation of the cytosolic AnxA2 to the cell surface.
27371724 0.98 ANXA2 and S100A10 genes were both up-regulated upon contact and ingestion of fungal cells by brain endothelial cells.
0.97 ANXA2's subcellular ligand, S100A10, is down-regulated in murine brain endothelial cells, there is both a decrease in phagocytosis and significant increase in the capsule size of cryptococcal cells.
0.95 ANXA2- and S100A10-deficient cells could reflect the fact that there is reduced damage to fungal cells from weaker oxidative fluxes in Anxa2-/- phagolysosomes, thus allowing them to express larger capsules.
0.93 ANXA2 and S100A10 are involved in a pathway that influences C. neoformans capsule growth.
27740735 0.98 annexin A2 or S100A10 have increased microvascular fibrin deposition in multiple organs suggesting that, unlike Plg-RKT, the annexin A2-S100A10 plasminogen receptor plays a key role in baseline plasmin-mediated fibrin surveillance and clearance.
0.98 annexin A2-S100A10, enolase-1, histone 2B, TATA-binding protein interacting protein, alphaMbeta2, and Plg-RKT, are expressed on the cell surface of monocytoid cells.
0.98 annexin A2-S100A10, enolase-1, histone 2B, and Plg-RKT) and multiple plasminogen receptors (annexin A2, enolase-1, histone 2B) are targets of autoantibody production in the context of autoimmune diseases.
0.91 S100A10 (in complex with annexin A2 within the annexin A2 heterotetramer) and Plg-RKT (see below), as well as, surprisingly, proteins with a normally intracellular location and function including cytoplasmic proteins (alpha-enolase, cytokeratin 8, actin) and nuclear proteins (TIP49a and histone H2B).
20607799 0.98 annexin A2 molecules bind with two molecules of S100A10, a member of the S100 family of proteins, to form a heterotetramer, which increases the affinity of annexin A2 for phospholipids and calcium promoting membrane binding.
0.98 annexin A2/S100A10 heterotetramer on the surface of endothelial cells is to promote normal fibrinolysis by acting as a co-receptor for plasminogen and tPA thereby greatly increasing the efficiency of plasminogen activation by tissue plasminogen activator.
0.97 annexin A2 in tumor cells and proliferating endothelial cells and thus it is reasonable to conclude that increased annexin A2/S100A10 heterotetramer on the surface of endothelial cells in new vessels is the basis for the ability of TM601 to home to the neovascularization regardless of its route of administration.
20816723 0.98 p11 (S100A10, Annexin 2 light chain) is a member of the S100 calcium binding protein family, which regulates many cellular processes in response to intracellular calcium changes.
0.98 Annexin II disrupts p11 binding, while the activation of a protein phosphatase by PKA and subsequent dephosphorylation of the same residue may allow coupling of the p11 localisation to the Ca2+ and cAMP-dependent cellular signalling pathways.
0.96 p11 present intracellularly, exists as a heterotetramer (A2t), composed of two identical annexin II heavy chains.
23193360 0.98 annexin A2 and p11 may have exposed lysine residues that are accessible to the lysine binding "kringle" domains of both tPA and plasminogen.
0.98 AnxA2-/- mice, which demonstrate low to nondetectable p11 expression, treatment with bortezomib, a proteasome inhibitor, restored p11 expression, verifying its regulation via a proteasome-linked pathway in vivo.
0.90 p11 as the key ligand interaction site and annexin A2 as the molecule that anchors it to the plasma membrane, another proposes annexin A2, in complex with p11, as the ligand binding site.
28652618 0.98 Annexin A2 is anchored at the plasma membrane as a heterotetrameric complex with S100A10.
0.98 annexin A2, in association with S100A10, regulates the proteolytic activity of plasmin, leading to hydrolysis and remodeling of the extracellular matrix (ECM) and activation of matrix metalloproteases in tumor invasion.
0.98 annexin A2-mediated tumor cell invasiveness is attributable to the generation of extracellular plasmin through modulation of S100A10 enzyme activity.
28694388 0.98 S100a10-/- mice, generated via homologous recombination (Fig. 3, A-C), showed slightly decreased ANXA2 expression, whereas S100A10 protein was almost undetectable in the Anxa2-/- lung (Fig. 3 D), reflecting our previous finding that ANXA2 stabilizes S100A10 in ECs by masking a polyubiquitination site that directs S100A10 to the proteasome for degradation.
0.94 Anxa2-/-, but not S100a10-/-, mice, which mimicked the wild-type (Fig. 3 G).
0.89 ANXA2 to promote pulmonary vascular integrity does not require expression of S100A10.
15819996 0.98 Annexin A2 is controlled by sequestration of the AnxA2/p11 complex modulated by phosphorylation and by a nuclear export signal found in the AnxA2 3-12 region.
0.98 Annexin A2 in the nucleus, that appears not to involve binding of p11, has been suggested by its purification as part of a primer recognition protein complex that enhances DNA polymerasealpha-activity in vitro.
21572519 0.98 ANXA2Y23A may sequester all of the S100A10/p11 in the cytosol, thereby conferring a dominant negative effect.
0.94 ANXA2Y23A can still bind to its partner S100A10/p11 in the cytosol, but not in the cell membrane (Figure S5).
25597631 0.98 S100A10 and S100A11), annexin A2 is known to bridge disparate membranes and promote fusion.
0.97 annexin A2 and two of an S100 protein, either S100A10 or S100A11.
18675323 0.98 S100a10, S100a11, S100a13 and S100a16, respectively) as well as their interacting proteins, annexin A2 and A3 (Anxa2 and Anxa3, respectively) are also increased in the intermediate phase.
19273183 0.98 annexin A2 heterotetramer, composed of annexin A2 and S100A10, is a co-receptor for plasmin and regulates plasmin activity.
19536308 0.98 Annexin A2 can form heterotetrameric complexes on the surface of endothelial cells with the annexin A2 light chain (called S100A10 or p11), and this stimulates generation of t-PA dependent plasmin.
21440088 0.98 Anxa2-/- mice express reduced levels of endothelial cell p11.
23032875 0.98 p11 (S100A10, annexin II light chain), which recruits 5-HT1BR (and 5-HT4R) to the cell surface.
23483454 0.98 AnxA2-/- mice, which demonstrate low to nondetectable p11 expression in most cells, treatment with bortezomib, a proteasome inhibitor, restored p11 expression in lung tissue, thus verifying that p11 is regulated via polyubiquitination in vivo.
26527544 0.98 AnxA2 endosomal binding is associated with increased S100A10 recruitment, and the heterotetrameric complex (AnxA2-S100A10) serves in the pro-inflammatory process.
31337068 0.98 AnxA2 proteins form a heterotetrameric complex with p11, a member of the S100 protein family, at the plasma membrane and intracellular compartments, while only small amounts of AnxA2 monomer are present in the cytosol, endosomes and nucleus.
31817350 0.98 Annexin A2 (AnxA2) is a 36 KD multi-compartmental protein that exists as a monomer or a heterotetrameric complex with the S100A10 (P11).
26885373 0.97 ANXA2 is the plasminogen receptor protein S100A10.
0.97 ANXA2m that exposes a hydrophobic residue in its N terminus, allowing ANXA2m to bind a S100A10 dimer.
0.93 ANXA2 bind to the S100A10 protein to form the ANXA2t. Since ANXA2t is unable to activate TLR2, we hypothesized that the N-terminus of ANXA2 was sufficient for signaling through TLR2, and that the first 15 N terminal amino acids were required for TLR2 activity.
27616678 0.97 P11, also known as S100A10, calpactin I light chain, or annexin II light chain, is a protein that forms a heterotetramer complex with annexin A2 (Anxa2) (Gerke et al., 2005; Oh et al., 2013).
0.97 p11/Anxa2 heterotetramer complex is involved in the organization of lipid microdomains on the cell membrane, bundling of actin filaments and cytoskeleton scaffolding, membrane trafficking, and fibrinolysis (Babiychuk and Draeger, 2000; Menke et al., 2005; Hayes et al., 2006; Surette et al., 2011).
0.95 p11/Anxa2 system is involved in many diseases, such as thrombosis, atherosclerosis, retinopathy, pain perception, and cancer, as well as in neuropsychiatric diseases (Hedhli et al., 2012).
19607921 0.97 p11, the light chain of annexin II, as a novel regulatory factor for NaV1.8.
20107310 0.97 annexin 2 and p11, was reduced.
24303218 0.97 Annexin A2 has been shown in different systems to affect neuronal ion channels and neuronal functioning, either directly or through its interaction with p11.
24725970 0.97 P11 is best known for its role as a regulator of surface expression of membrane proteins such as serotonin receptors 5HT1b and 5HT4, ion channels, and its protein partner Annexin A2.
26839892 0.97 S100A10 or p11) functions as a ligand of annexin II (annexin II2 : p112).
22073239 0.96 Annexin 2 and S100A10 that complex with CFTR enabling its function.
27457815 0.96 p11 (also known as annexin II light chain, S100A10), a multifunctional protein binding to 5-HT receptors, in layer II/III neurons of the prelimbic cortex (PrL), as well as depression-like behaviors, both of which are reversed by selective serotonin reuptake inhibitors (SSRIs) and the tricyclic class of antidepressant (TCA) agents.
30675195 0.96 S100A10 expression caused by ANXA2 knockdown resulted in decreased tumor growth and proliferation in GL621 mouse glioma cells.
21335281 0.94 annexin 2 and p11, and showed little surface expression of Plg.
0.80 annexin 2, p11 and H2B indicate that these tailless Plg-Rs account for the preponderance of the Plg binding capacity of monocytoid cells of either murine or human origin although the effects of antibodies to other Plg-Rs have not been directly compared.
26444699 0.94 Axna2 is a heterotetramer consisting of two Axna2 and two S100A10 (S100 calcium binding protein A10) molecules.
0.89 S100A10, the binding partner of Axna2 heterotetramers, caused implantation failure in mice.
23296618 0.90 S100A10-annexin A2 interaction have not been validated in vivo but their predicted clinical uses include angiogenesis and cancer metastasis therapy.
26423360 0.87 annexin 2 light chain p11 has been shown to promote Nav1.8 translocation to the plasma membrane, axonal localization of Nav1.8 in sciatic nerve and dorsal root or in cultured DRG neurons has not yet been examined in the p11 knockout mice.
26206886 0.80 Anxa2, S100a4, S100a10 and Capn3, were visualized in Volcano plots in five different comparisons (Supplementary Material, Fig. S2); Myof, Anxa1, Anxa2, S100a4 and S100a10 were significantly upregulated by Fst overexpression while Capn3 was significantly downregulated by Fst overexpression.
21995826 0.77 AnxA2 bound to one subunit of 3-phosphoglycerate kinase) or a heterotetramer (two subunits of AnxA2 linked to two subunits of S100A10) (AIIt).
25560297 0.67 Annexin2/S100A10 heterotetramer, natriuretic peptide receptor, dysferlin, calpain 3, and S100B.
19261867 0.66 annexin II light chain (p11) between residues 74-103 of the N-terminus of Nav1.8.
27446808 0.60 annexin II/p11 in homing and engraftment to the bone marrow.



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