Publication for Hspd1 and Hspe1

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
mmu	Hspd1	heat shock protein 1 (chaperonin)	15510			[link]
mmu	Hspe1	heat shock protein 1 (chaperonin 10)	15528

Pubmed ID	Priority	Text
31428613	0.99	HSP60 is able to interact with different HSPs, such as HSP10, forming a complex that mediates protein folding, and with mitochondrial HSP70 (HSP70A), also known as mortalin, that have a role in cell proliferation and stress.
32317635	0.98	mHsp60 and its co-chaperonin mHsp10 assist the folding of mitochondrial-imported proteins, and correct misfolded polypeptides resulting from mitochondrial stress.
	0.98	mHsp60 and mHsp10 have also been implicated in a wide range of extra-mitochondrial and cytosolic activities, including the regulation of inflammatory cytokines, apoptopic processes, and carcinogenesis.
	0.97	mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins without the negative ATP binding inter-ring cooperativity of GroEL-GroES.
	0.97	mHsp60-mHsp10 football complex unable to progress through the reaction cycle and assist substrate-protein folding (Supplementary Fig. 7a).
	0.95	mHsp60-mHsp10 chaperonin system.
	0.94	mHsp60-mHsp10 chaperonin system forms alternating single and double ring complexes to assist protein folding, but the molecular details of this cycle are not fully understood.
	0.94	mHsp60 can also assemble into stacked back-to-back double-heptameric rings capped by a dome-shaped heptameric mHsp10 (GroES in the case of E. coli) co-chaperonin lid to form ATP-driven nanocages for a substrate-protein to fold in confinement.
	0.94	mHsp10 and mHsp60 eluted (Supplementary Fig. 7c, d) as oligomers with an apparent molecular weight of ~823 kDa, consistent with a stable double-heptameric ring, likely a football complex.
	0.94	mHsp60 and the S464C variant formed stable football complexes with mHsp10, both S464R and S464R/K109E mHsp60 variants assembled into single rings without evidence of higher oligomeric species (Fig. 6a).
	0.94	mHsp60 complexes coexist in the reaction cycle of the human mHsp60-mHsp10 chaperonin system.
	0.93	mHsp10 and liberate the folded substrate-protein, it provided structural evidence for the formation of mHsp60-mHsp10 football complexes.
	0.93	mHsp10, consistent with reports showing that mHsp60 binds mHsp10 in the presence of ATP, AMPNP and ADP-BeF3, but not ADP and ADP-AlF3.
	0.92	mHsp60-mHsp10 football complexes.
	0.90	mHsp60-mHsp10 football complex mimicking the ATP-bound ground-state intermediate and the changes in symmetry and at the inter-ring interface resulting from ATP hydrolysis.
	0.89	mHsp60-mHsp10 chaperonin reaction cycle.
	0.89	mHsp10 protomer adopts the canonical seven-strand beta-barrel structure and exposes a flexible loop sequence of twenty residues (mobile loop) that mediates the interaction with helices H and I of the mHsp60 apical domains.
	0.89	mHsp60-mHsp10 structures were occupied by ADP, indicating that under our specimen preparation conditions ATP hydrolysis had occurred rapidly.
	0.85	mHsp60-mHsp10 folding activity.
	0.84	mHsp60 and mHsp10 assembled primarily into football complexes (Fig. 1b) accounting for ~70% of the particles, followed by half-football complexes (~30% of the particles) (Supplementary Fig. 2b).
	0.84	mHsp60-mHsp10 chaperonin system, in vitro, or in bacteria.
	0.83	mHsp60-mHsp10, however, points to minimal contacts holding the two mHsp60 rings together (Fig. 4b), in a manner consistent with the lack of inter-ring negative cooperativity observed in biochemical experiments.
	0.79	mHsp60-mHsp10.
	0.70	mHsp60-mHsp10 complexes representing a ground-state particle ready for folding, the ADP:BeF3-bound double-ring mHsp6014-(mHsp107)2 football, its apparent successor state, an ADP-bound mHsp6014-(mHsp107)2 football, and an ADP-bound single-ring mHsp607-mHsp107 half-football, at resolutions ranging from 3.8 to 3.1 A. Complemented with in vitro and in vivo assays with obligate double and single-ring mHsp60 variants, our work provides a structural basis for active football and half-football complexes coexisting in the reaction cycle of human mHsp60-mHsp10.
	0.59	mHsp60-mHsp10, i.e., assisted folding by way of footballs or half-footballs.
	0.55	mHsp60-mHsp10 complexes (Fig. 2).
23226518	0.98	mHsp60 to mHsp10.
	0.98	mHsp60 and mHsp10, are key players in the homeostasis of mitochondria since they mediate the folding of proteins in the matrix, an environment containing only a limited number of chaperones (in the human mitochondria there are only one Hsp60, one Hsp70 and no ClpB homologues).
	0.97	mHsp60 and mHsp10) in a wide range of extra-mitochondrial activities.
	0.97	mHsp60 can stimulate human leukocytes and vascular endothelial cells to produce pro-inflammatory cytokines, while mHsp10 was shown to stimulate the production of anti-inflammatory cytokines and suppress the production of pro-inflammatory cytokines.
	0.97	mHsp60 and mHsp10 were found to change their expression pattern in tumor cells.
	0.97	mHsp60 is capable of complementing a bacterial GroEL depletion strain, when co-expressed with mHsp10, it is incapable of functionally interacting with, or even binding to, GroES, the bacterial co-chaperonin.
	0.97	mHsp60, showed the same preference for mHsp10 co-chaperonin as the wild-type mHsp60.
	0.97	mHsp60 can compensate for the decreased affinity of the L33A mHsp10 mutant to chaperonins.
	0.97	mHsp60 and mHsp10 affect processes that are not related directly to protein folding, such as apoptosis and inflammation.
	0.97	mHsp60 mutants that are functional with GroES lent insight into the molecular basis for the exclusive interaction between mHsp60 and mHsp10.
	0.96	mHsp10 can be explained by the concurrence of two distinct processes: monomerization of the unstable mHsp60 oligomers and slow dissociation of a very stable and non-functional complex formed between E321K and mHsp10.
	0.95	mHsp60) and the co-chaperonin (known in bacteria as GroES and in mammals mHsp10).
	0.95	mHsp10 stems from a generally weak affinity of mHsp60 for co-chaperonins relative to GroEL, with a correspondingly high binding affinity of mHsp10 to chaperonins compared to other co-chaperonin homologs.
	0.95	mHsp60 with its co-chaperonin, mHsp10, we adopted an unbiased directed evolution approach to identifying the amino acids responsible for this specificity.
	0.95	mHsp60, from being functional only with mHsp10 to being functional only with GroES.
	0.95	mHsp60 to bind mHsp10.
	0.94	mHsp60 mutants exhibited altered specificity, with a preference for GroES over mHsp10 in vivo.
	0.93	mHsp60 to all co-chaperonins, thereby enabling the mutant to bind GroES with moderate affinity, but leading to a very tight and non-functional binding to mHsp10, which was suggested to have a relatively high affinity for chaperonins compared to other co-chaperonins.
	0.90	mHsp60-mHsp10 pair to complement a depletion of the bacterial chaperonins in E. coli, we developed a screen which uses selective pressure to isolate mHsp60 mutants that are able to function when assisted by the bacterial co-chaperonin, GroES.
	0.90	mHsp60 and mHsp10 in the presence of ADP, it was suggested that following ATP hydrolysis, when ADP occupies the cis ring, the complex between mHsp60 and mHsp10 dissociates spontaneously, without the requirement for an allosteric signal induced by ATP-binding to the trans ring.
	0.89	mHsp60-mHsp10 pair, previous studies showed that mammalian mHsp10 binds to mHsp60 only in the presence of ATP, but not ADP.
	0.83	mHsp10 is formed, as opposed to the dynamic and functional complex that is formed between the wild-type mHsp60 and mHsp10.
	0.81	mHsp60 to functionally interact with the low-affinity co-chaperonin, GroES, and with the low affinity mHsp10 mutant, L33A.
	0.72	mHsp10 (by 67% and 53%, respectively) and that of mHsp60 was inhibited, as expected, only by mHsp10 (by 49%) (Table 1).
19402213	0.98	HSP60 with Hsp10 revealed that nitrated HSP60-Hsp10 complexes partly preserve their responsiveness to protein substrates.
	0.97	HSP60 with HSP10 showed that increasing HSP60 nitration led to a progressive loss of the inhibitory effect of Hsp10 on the HSP60 ATP hydrolase activity.
	0.97	HSP60-HSP10 chaperone system may prevent protein misfolding under stress conditions and facilitate the unfolding, refolding and proper assembly of nonnative proteins, thus preventing their aggregation.
	0.96	HSP60 (Figure 4B) that correlated with a significant decrease in the hydrolysis rate of ATP in the presence or absence of the co-chaperonin Hsp10 and/or protein substrate in the form of denatured mMDH (Table 2).
	0.95	HSP60 ATPase activity observed in our study implicates a fundamental loss of function that could include one or more of the following: (i) ATP binding; (ii) ATP hydrolysis; and (iii) interactions between amino acids involved in crucial conformational shifts, binding of HSP10, and/or binding of substrate.
	0.94	HSP60 not only caused a general decrease in the ATP hydrolysis activity but altered the interaction of HSP60 with Hsp10 and to a lesser degree with substrate proteins.
	0.94	HSP60 and HSP10 manifested in the nitrative loss of HSP60 ATPase inhibition by HSP10 in the absence of protein substrate; and (ii) the decreased stimulatory effect of denatured mMDH on the ATPase activity of the HSP60-HSP10 complex.
	0.93	HSP60 even in the absence of HSP10 as it promoted the inhibition of nitrated HSP60.
24223161	0.98	Hsp60 and Hsp10, which may mediate both Fhit stability and its mitochondrial localization; once in the mitochondria, Fhit binds and stabilizes ferredoxin reductase (Fdxr), leading to modulation of the production of reactive oxygen species (ROS), an early step in Fhit-induced apoptosis.
	0.98	Hsp10/Hsp60 complex was involved in the translocation of Fhit protein into mitochondria, where its interaction with Fdxr was involved in modulation of production of reactive oxygen species, the earliest step in Fhit-mediated apoptosis.
	0.93	Hsp10/Hsp60 and ferredoxin reductase (Fdxr) among other mitochondrial proteins.
27523387	0.98	Hspd1 (p<0.05) in mouse oocytes and Hspe1 in mouse granulosa cells (p<0.05).
	0.95	Hspd1 in oocytes and Hspe1 in granulosa cells, while Clpp and Dnaja3 were unchanged (Figures 4 and 5).
	0.79	Hspd1 demonstrates increased expression in aged mouse oocytes, and Hspe1 demonstrates increased expression in aged mouse granulosa cells
29755410	0.98	Hsp60 and Hsp10, strengthening the hypothesis that increased mitochondrial chaperones expression is beneficial for insulin sensitivity.
	0.98	Hsp60 and its co-chaperone Hsp10 are required for folding nuclear-encoded mitochondrial matrix proteins and are key players of the UPRmt by propagating ATP-dependent refolding of misfolded proteins.
	0.96	heat shock protein 60 cooperates with its co-chaperone Hsp10 in order to promote correct protein folding.
30200516	0.98	Hsp60 is a protein that, together with its co-chaperone Hsp10, is considered essential for mitochondrial protein folding.
	0.83	Hsp10 from the Hsp60/Hsp10 complex with a significant difference in the activities observed with the prokaryotic GroEL/GroES system, which is not significantly affected by mizoribine.
	0.50	Hsp60 was only recently resolved and the models for the Hsp60 folding machine are still under debate considering: the bullet versus football complex with Hsp10 co-chaperones; one-ring heptamers versus two-ring tetradecamers; the significant differences between crystal and in solution structures.
19086848	0.98	Hsp60/Hsp10 are Fhit interactors, suggesting a direct role for Fhit in stress responses.
	0.88	Hsp60-Hsp10 complex.
21060842	0.98	Hspd1 and Hspe1 function to refold proteins once they have been translocated to the mitochondrial matrix.
	0.96	Hsp60/Hspd1 and GroES/Hsp10/Hspe1 partners, and 2) the Cytosolic chaperonin containing t-complex (Cct/TRiC) which function by encapsulating proteins and domains of proteins up to 220 kD in size to facilitate folding.
21946932	0.98	HSP-10 and HSP-60 are potential antigens (Ag) in atherosclerosis that induce IL-12 and IL-23 expression by dendritic cells (DCs), which have been demonstrated to be present within atherosclerotic regions.
	0.95	HSP-10 and HSP-60 may serve as one of the potential Ags for Th17 cell expansion.
23293686	0.98	HSPE1 and its co-chaperonin HSPD1, are bound by HSF1 in both cell types.
	0.62	HSPE1, HSPD1 and HSPA8 (Figure 1B, Figure S1).
25543897	0.98	Hsp60 and Hsp10 fold and assemble proteins that are imported into the mitochondria and refold damaged mitochondrial proteins.
	0.98	Hsp60, Hsp10, mtHsp70, ClpP, Lonp1 and Ubl5 form a tight coexpression network in mice GRPs and human populations, suggestive of their transcriptional control.
26404765	0.98	HSP10, HSP60, and CLPP (data not shown), is indicative of the UPRmt (Fig. 6B).
	0.91	Hspe1 (HSP10), but not Hspd1 (HSP60) (n = 6).
26498839	0.98	HSP60, HSP70, and HSP10 are increased in relative abundance in aged EDL.
	0.97	HSP60, HSP70, and HSP10, was also increased in aged EDL (Table S2).
26795070	0.98	Hsp60, a molecular chaperone that assists protein folding in mitochondria together with its cochaperone Hsp10.
	0.98	Hsp60 nitration in hyperglycemia not only causes a significant decrease in the ATP hydrolysis rate but also altered the interaction of the protein with its cochaperone Hsp10, impairing Hsp60 folding activity.
27056903	0.98	HSP60 works together with its co-chaperone HSP10 to assist proper folding and assembly of mitochondrial proteins in response to oxidative stress.
	0.97	Hsp10 and Hsp60), assists nascent polypeptides to reach a native conformation.
27166255	0.98	Hsp60 and Hsp10 take Fhit protein into the mitochondrion where it binds some mitochondrial proteins, including Fdxr; this protein complex induces the generation of reactive oxygen species (ROS) which, in turn, triggers apoptosis of Fhit-negative cancer cells.
	0.98	Hsp10, Hsp60, and ferredoxin reductase which underlies and supports the role of Fhit in apoptosis through the generation of free radicals in mitochondria.
27786175	0.98	HSP60, its co-chaperone HSP10 and proteases like ATP-dependent caseinolytic peptidase proteolytic subunit homologue (CLPP).
	0.98	Hsp10, ClpP and Chop upon Hsp60 knockout, reflecting the effects seen in vivo (Fig. 4f).
29082112	0.98	HSP60-HSP10.
	0.98	HSP-60, HSP-6, HSP-10 and CLPP-1.
29132502	0.98	Hsp60/Hspd1), 10 kDa heat shock protein (Hspe1) and mitochondrial stress-70 protein (mtHsp70/Hspa9).
	0.95	HSPD1, HSPE1, and HSPA9 in all five knockouts (Figure 5D; Figure 5:figure supplement 1B; box plots in Supplementary file 8).
18948619	0.98	Hsp10 and Hsp60, which have been found to modulate DOX-induced mitochondrial apoptosis signaling in neonatal cardiomyocytes.
21603190	0.98	Hsp10, Hsp60, and Hsp72), ubiquitin, uric acid, and HMGB-1, have recently been shown to modulate the host inflammatory response in vitro.
22073363	0.98	hsp10 is a eukaryotic cpn10 homologue and, therefore, together with cpn60 is essential for mitochondrial protein biogenesis.
22485093	0.98	HSP10 production is the cause or the consequence of AIP progression, but HSP10 consistently inhibits LPS-induced TLR4 signaling by interacting with HSP60 in the extracellular milieu and inhibits LPS-induced secretion of the pro-inflammatory cytokines, TNF-alpha, IL-6, and the pro-inflammatory chemokine regulated upon activation, normal T cell expressed and secreted (RANTES) and anti-inflammatory cytokine IL-10 (Johnson et al.,).
22559204	0.98	Hspd1 and Hspe1 all exhibited significantly (P < 0.05) different expression in bystander cells at all times evaluated.
23870130	0.98	HSP60 and HSP10 and the protease CLPP.
25762445	0.98	HSP60, HSP10 and mtHSP70 during heat shock in mouse cells, and SSBP1, which localizes mostly in the mitochondria, enhances their expression by potentiating the transcriptional activity of HSF1 (Figs 6, 7).
27684481	0.98	Hsp60, Hsp10, and mtHsp70 are organelle-specific biomarkers that are considered to reflect mitochondria stress.
28943839	0.98	Hsp60 associated with Hsp10, as well as the mitochondrial Hsp70 (mtHsp70) and the mitochondrial Hsp90 analog TRAP1.
30013058	0.98	HSPD1, HSPE1) as determined by MSigDB (p > 5.88e-12, FDR 7.35e-11, Supplementary Table 3, Fig. 5d).
30650373	0.98	Hsp60, Hsp40, and Hsp10 (Figure 2A).
31601784	0.98	HSP60 together with HSP10 is generally recognized to form the mitochondrial molecular chaperonin and promote protein folding.
27992860	0.97	HSP60/HSP10 complex is critical for proper protein folding as loss of function leads to an accumulation of protein aggregates.
	0.97	HSP60/HSP10 are pro-apoptotic.
	0.96	HSP60/HSP10 chaperonin system interacts with the incompletely folded protein.
	0.86	HSP60, HSP10, was also found to decrease with advanced age in two mouse brain models, from 12 - 24 months and 5 - 24 months old.
28008398	0.97	mHsp60, hydrolysis of ATP to ADP was proposed to cause a drastic decrease in co-chaperonin binding, allowing rapid dissociation of the mitochondrial Hsp10 and release of the encapsulated protein (Nielsen and Cowan,).
	0.88	mHsp60-mHsp10 structure shows ADP in all the 14 sites, a conformation which cannot exist for GroEL-GroES due to the strong inter-ring negative cooperativity of nucleotide binding.
31423721	0.97	Hsp60 and Hsp10, confirming that this drug is indeed effective on Snell fibroblasts and activates mtUPR as expected (Figure S1).
	0.96	Hsp60 and Hsp10, and nicotinamide riboside treatment starting at old age (22-24 months), which reverses this decline in the mtUPR pathway, induces neurogenesis and increases mean lifespan of old mice (Zhang et al., 2016).
26504810	0.97	HSP60, together with HSP10, refold all proteins imported into the mitochondrial matrix and facilitate the restoration of unfolded or misfolded matrix proteins under normal and stressed environments; hence, they are vital for maintaining mitochondrial functions, including ATP synthesis.
27630992	0.97	HSP60/HSP10 complex are essential in organisms from bacteria to mice (Cheng et al.,; Fayet et al.,; Perezgasga et al.,; Christensen et al.,).
28851515	0.97	HSP60/HSP10 chaperonin complex is a major component in the UPRmt.
25479961	0.96	Hsp10, Hsp60, and others) and proteases (Lon, AAA proteases) needed for refolding or degrading individual proteins, mitochondrial integrity is maintained through the regulation of protein import via the TOM/TIM complex and protein redistribution across the network via fusion and fission and through mitophagy and biogenesis, key determinants of mitochondrial turnover.
26805490	0.96	HSPD1 were found to be significantly higher in both MSC specimens, while HSP90AB1, HSPB1 and HSPE1 were significantly increased only in MSC1 cells compared to HS68 fibroblasts.
28955973	0.96	heat shock protein 60 (HSP60) and 10 (HSP10) during fasting differed between the two genotypes, highlighting the importance of these proteins in VLCAD deficiency.
19096088	0.95	HSP60 and HSP10 are proapoptotic.
21819105	0.94	Hsp60 or Hsp10, proteins known to associate with HspA9, were found equally distributed in immunoprecipitation eluates collected from DJ-1 knockout and wild-type extracts.
26945277	0.94	HSP60 and HSP10, and the mitochondrial protease ClpP, have not been tested in HSCs, but these experiments will be informative in understanding the role of the UPRmt-mediated metabolic checkpoint in regulating HSC quiescence.
29851234	0.94	Hspd1, Hspe1, and Dnaja3, were also significantly lower in Clpp -/- oocytes (Supporting Information Figure S5).
30089252	0.90	Hsp60 and mRNA levels of Hsp10, ClpP, and Yme1l, markers of the mtUPR, were normal in Drp1iDeltab/iDeltab brains (Figures S3A-S3C).
20059764	0.89	Hspe1, and Hspd1.
28542188	0.72	HSP60/HSP10), CCT (TRiC), DNAJ (HSP40) and HSPB (small HSP).
25858032	0.64	HSP60, HSP56, HSP40, HSP10, and cyclophilin A. Prolonged 'rafenib/sildenafil treatment killed tumor cells and also rapidly decreased the expression of: the drug efflux pumps ABCB1 and ABCG2; and NPC1 and NTCP, receptors for Ebola/Hepatitis A and B viruses, respectively.