Publication for Tor1a and Tor1b

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
mmu	Tor1a	torsin family 1, member A (torsin A)	30931			[link]
mmu	Tor1b	torsin family 1, member B	30934

Pubmed ID	Priority	Text
32202496	0.98	torsinA mutants coincides with lower levels of torsinB during early brain maturation.
	0.98	torsinB removal increases the susceptibility of multiple cortical neuron populations to torsinA LOF.
	0.98	torsinB in the tissue selectivity and timing of torsinA-related cell biological phenotype of NE budding.
	0.97	torsinB in torsinA null non-neuronal cells recapitulates the 'neuronal-like' NE budding phenotype.
	0.97	torsinA and torsinB causes NE budding in neuronal and non-neuronal (e.g. glia) cells, and overexpressing torsinB significantly reduces NE budding in torsinA null developing neurons in vitro.
	0.97	Tor1b-/- mice appear normal, these data suggest that torsinB expression is an essential contributor to neuronal viability on the torsinA null background.
	0.97	torsinB overexpression significantly suppresses a torsinA LOF cellular phenotype in vitro.
	0.97	torsinB can compensate for torsinA LOF.
	0.97	torsinA LOF and torsinB levels is reminiscent of spinal muscular atrophy (SMA), a disease linked to LOF of the SMN1 gene.
	0.97	torsinB levels bidirectionally modulate the severity of torsinA LOF, worsening mouse phenotypes when reduced and attenuating them when overexpressed.
	0.96	torsinB in DYT1 models (Tor1a-/- or Tor1aDeltaE/-) causes a dose-dependent worsening of behavioral and neuropathological phenotypes.
	0.96	TorsinB overexpression did not significantly alter torsinA expression in brain lysates, indicating that there is not a direct regulatory relationship between levels of these proteins (Figure 3:figure supplement 2A-B).
	0.96	torsinB can significantly ameliorate torsinA LOF phenotypes, even when torsinA is absent from the entire central nervous system.
	0.96	torsinA and activate torsinB overexpression in the same spatiotemporal pattern, demonstrating a cell autonomous rescue of torsinA LOF-mediated neurodegeneration.
	0.95	TOR1A gene encoding torsinA. Prior work demonstrates that torsinA and its paralog torsinB have conserved functions at the nuclear envelope.
	0.95	torsinB as a potent modifier of torsinA LOF phenotypes and suggest that augmentation of torsinB expression may retard or prevent symptom development in DYT1 dystonia.
	0.95	torsinB reduction dose dependently worsens DeltaE torsinA LOF-mediated phenotypes.
	0.95	torsinB cause a dose-dependent worsening of neuropathological and motor abnormalities in multiple DYT1 models, including one containing the pathogenic DeltaE disease mutation.
	0.95	torsinB overexpression prevents both striatal ChI degeneration and twisting movements further strengthens the relationship between dysfunction of these cells and DYT1-related abnormal movements.
	0.95	torsinB in DYT1 dystonia and demonstrate that torsinB expression is a bidirectional modifier of torsinA LOF phenotypes.
	0.94	torsinB overexpression would rescue mouse phenotypes in the presence of DeltaE torsinA.
	0.93	torsinB levels would modulate motor and neuropathological phenotypes of DYT1 mouse models.
	0.93	torsinA and torsinB expression in CNS and peripheral tissues.
	0.92	torsinB to potently suppress DYT1-related motor and neuropathological phenotypes.
	0.91	torsinB levels causes a dose-dependent worsening whereas torsinB overexpression rescues torsinA LOF-mediated abnormal movements and neurodegeneration.
	0.90	torsinB from the ROSA26 locus dramatically reduces the emergence of motor and neuropathological phenotypes in two DYT1 models.
	0.90	torsinB expression in the context of torsinA LOF, and the developmental- and dose-dependent effects of torsinB expression level, we next explored whether enhancing torsinB levels could suppress or prevent torsinA LOF phenotypes.
	0.89	torsinB overexpression can rescue torsinA LOF phenotypes in the presence of DeltaE torsinA.
	0.88	TorsinB overexpression rescues DeltaE torsinA phenotypes.
	0.88	torsinB to DYT1 pathogenesis.
	0.87	torsinB expression levels impact the onset or severity of abnormal movements or neuropathological features in DYT1 mouse models.
	0.87	TorsinB deletion worsens torsinA-related motor and neuropathological phenotypes.
	0.85	torsinB is a genetic modifier of torsinA LOF disease-related phenotypes and suggest that enhancing torsinB function may be a viable therapeutic strategy in DYT1 dystonia.
	0.83	torsinB may be an effective therapeutic target in DYT1 dystonia.
	0.78	torsinA does not blunt the ability of torsinB overexpression to rescue torsinA LOF phenotypes.
	0.78	torsinB as a target for DYT1 dystonia therapeutics.
	0.76	TorsinB overexpression prevents abnormal twisting in DYT1 dystonia mouse models
	0.76	TorsinB overexpression rescues DeltaE torsinA phenotypes
	0.70	torsinB to suppress motor phenotypes in a validated DYT1 model.
	0.65	TorsinB deletion worsens torsinA-related motor and neuropathological phenotypes
	0.59	torsinB as a modifier of torsinA LOF, we first assessed whether torsinB null mice exhibit any pathological phenotypes.
	0.56	torsinA and torsinB with Emx1-Cre (Emx1(A+B)-CKO, Figure 1:figure supplement 2A) does not cause overt brain structural abnormalities at birth: cortical thickness and the number of CTIP2+ cells do not differ significantly from littermate controls at postnatal day 0 (P0) (Figure 1:figure supplement 2B-C).
27653693	0.98	torsinB also correlate with NE bud formation in differentiating DYT1 embryonic stem cells, and overexpression of torsinA or torsinB rescues NE bud formation in this system.
	0.98	torsinB as a regulator of the opening and closing of the neurodevelopmental window for NE budding in torsinA mutant mice.
	0.98	torsinB as a potent molecular modifier of torsinA-dependent NE budding, demonstrating its ability to strongly influence both the opening and closing of the neurodevelopmental window for this process, and show that overexpression of torsinB can suppress NE bud formation in an in vitro model of DYT1 dystonia.
	0.98	torsinB on the torsinA null background dramatically lengthened the neurodevelopmental window, causing NE buds to form in migrating neurons (Fig. 3E-H) and to persist in mature neurons - maturational states in which NE buds are never seen in torsinA null mice.
	0.98	torsinA or torsinB to suppress NE budding in immature neurons contrasts with our previous work demonstrating that overexpression of these proteins increases NE budding in more mature primary neuronal cultures, further highlighting a critical role for developmental timing in torsin protein family function emphasized by our in vivo studies.
	0.98	torsinA, torsinB, LAP1 and LULL1 demonstrates a unique divergence of torsinB expression levels during neural and cardiomyocyte differentiation.
	0.97	torsinB protein, while ablating torsinB from torsinA null neurons prevents budding resolution and causes lethal neural dysfunction.
	0.97	torsinA paralog, torsinB. We reported previously that in vitro torsinA and torsinB have conserved function at the NE and that in torsinA null tissue, levels of torsinB strongly influence the susceptibility of different cell types to the formation of NE buds (e.g., in neuronal vs. non-neuronal cells).
	0.97	torsinB in the developmental regulation of neuronal NE budding, and suggest a potential molecular mechanism underlying the selective vulnerability of immature neurons to torsinA loss of function.
	0.97	torsinB levels as a physiological mechanism modulating the window of vulnerability to torsinA loss of function.
	0.97	torsinA and torsinB rescued NE budding phenotype in mutant neuronal EBs.
	0.96	DYT1 mutant mouse ES (mES) cells, and demonstrate that overexpression of torsinB (or torsinA) can rescue NE bud formation.
	0.96	torsinA-associated NE budding seen in vivo: neuronal cell specificity and autonomy, developmental dependence, and anti-correlation with levels of torsinB.
	0.96	torsinB can effect rescue is critical, because any therapeutic strategy based on increasing endogenous torsinA levels will necessarily increase DYT1 mutant torsinA - which could negate any beneficial increases from the wild type protein through dominant negative effects.
	0.96	TorsinB overexpression suppresses NE budding during the maturation of DYT1-mutant neurons
	0.95	torsinA-related NE budding, linking this process to a discrete neurodevelopmental window, and identify the developmental expression pattern of torsinB as a molecular mechanism governing the temporal window of neural susceptibility to torsinA loss-of-function.
	0.95	torsinB levels are low as NE buds accumulate (P0 to P7), and that torsinA and torsin B exhibit opposite changes in levels of expression as NE buds resolve (P7 to P28).
	0.94	torsinB is a potent modifier of torsinA phenotypes and a potential therapeutic target.
	0.93	torsinA paralog, torsinB. The developmental upregulation of endogenous torsinB levels corresponds to the disappearance of buds, and in mice null for both torsinA and torsinB, NE buds develop earlier (in migrating neurons) and persist into adulthood.
	0.93	torsinA and torsinB significantly decreased the percentage of nuclei with NE buds (by nearly 50%).
	0.93	torsinB can suppress NE bud formation in a novel in vitro model of DYT1 dystonia.
	0.93	torsinA and torsinB share a redundant function at the NE and that developmental window for NE budding reflects a time when aggregate torsin protein function (represented by the combination of torsinA and torsinB levels) dips below a critical threshold.
	0.91	Tor1b-/- mice, this finding is consistent with previous work indicating that torsinA and torsinB share conserved function.
	0.87	torsinA or torsinB could "rescue" NE budding.
	0.85	torsinA and torsinB protein in spinal cord (SC), pons, and cortex (Ctx) in Syn-dCKO mice.
	0.83	torsinA, GFP-torsinB, or GFP-torsin2A midway through neuronal differentiation.
	0.70	torsinB in modifying torsinA-related NE budding, we used nestin-Cre to conditionally delete these genes from neural progenitor cells (nestin double conditional knock out, herein "N-dCKO"; Fig. 3B).
	0.65	torsinB in neuronal NE budding, we used gene targeting to explore the consequences of Tor1b deletion, and the effect of altering torsinB function in the context of torsinA loss-of-function (Fig. S3).
	0.58	torsinB in this process, whether overexpression of torsinB can suppress NE bud formation in vivo, and if this will ameliorate the behavioral phenotypes in torsinA mutant mice
22611399	0.98	torsinA, torsinB, and torsin2) operate within the NE, making them candidates for involvement in nuclear-cytoskeleton links.
	0.97	torsinA and torsinB.
	0.94	torsinA and torsinB associate with each other and have a similar distribution in nonneuronal cells.
	0.91	torsinA, torsinB expression is temporally and spatially regulated, with torsinB expression in the developing brain peaking after that of torsinA. The low expression of torsinB relative to torsinA in the brain and the high expression of torsinB in other tissues may explain why the brain is selectively affected by mutant torsinA and why nonneuronal tissue are protected from torsinA dysfunction in DYT1 patients.
	0.89	torsinB, which has very similar characteristics to torsinA, the subcellular localization of torsin2 and torsin3 remains poorly characterized.
	0.78	torsinA, torsinB (85% similar to torsinA), torsin2, and torsin3 (67% and 61% similar to torsinA, resp.) (Figure 1).
24508913	0.98	torsinB from fibroblasts lacking torsinA also leads to abnormal nuclear envelope morphology, suggesting that torsinA and torsinB share redundant functions in conjunction with LAP1.
	0.95	torsinA is expressed at relatively higher levels in neuronal tissues whereas torsinB and torsin3 are expressed at higher levels in non-neuronal tissues.
	0.71	TorsinA is expressed at greater levels in neural tissues compared to non-neural tissues, whereas a strikingly opposite pattern is observed for torsinB. The expression pattern of torsin3a is similar to torsinB, whereas torsin2a is expressed at similar levels in all tissues examined.
26803745	0.98	TorA KO mice exhibited normal NEs, but upon siRNA treatment against TorsinB (TorB), these cells also exhibited the blebbing phenotype, establishing functional redundancy between the two Torsins.
	0.95	TorsinA and TorsinB.
28553638	0.98	TorsinA knockout mice, blebbing is restricted to a specific developmental window, and the resolution of the blebs in later stages is dependent on increasing expression levels of TorsinB (Tanabe et al.,).
	0.96	TorsinA knockout mice, additionally depleting TorsinB is sufficient to induce blebbing (Kim et al.,).
25739455	0.98	TorsinA phenotypes in mice are restricted to neurons, likely due to considerably higher expression levels of torsinB in nonneuronal tissues.
23028827	0.97	Torsin1a and Torsin1b isoforms primarily localized to the cytosol (figure 8A, B) in the mouse dopaminergic MN9D cell line.
	0.83	TorsinA and TorsinB have redundant functions, there is evidence that TorsinB may partially compensate for the functional effects of mutations in TorsinA: morphological abnormalities of the nuclear envelope in fibroblasts derived from DeltaE/DeltaE knock-in mice were exacerbated by loss of TorsinB. Consequently, it is possible that the single tor1 gene in zebrafish will prove advantageous for determining the role of Torsin1 in neurons, since loss-of-function phenotypes might not be mitigated by compensatory functions provided by closely related proteins.
22391119	0.97	Dyt1 DeltaGAG homozygous KI mice may be caused by malfunction of torsinA with incomplete compensation by torsinB, which is weakly expressed in neurons.
25425325	0.97	torsinA, blebs are only present in neurons, probably because of the high level of torsinB in non-neuronal cells.
22393392	0.96	torsinA and torsinB share redundant functions in multiple cell types, raising the possibility that torsinB influences disease penetrance.
	0.64	torsinA pathway include torsinB, which has redundant functions, and other torsinA-interacting proteins, including LAP1, LULL1 and printor.
26592310	0.96	TorsinB mRNA expression levels remain constant after P14, while TorsinA mRNA expression levels decrease, suggesting that TorsinA may play a more important role in early developmental stages.
	0.61	TorsinB has a tendency to form inclusions when overexpressed, while these inclusions are not seen with a similar level of TorsinA overexpression.
19214349	0.95	DQ1 and DQ2, when associated with the presence of anti-SSA/Ro and anti-SS-B/La autoantibodies.
19219532	0.95	DQ1 and DQ2, when associated with the presence of anti-SS-A/Ro and anti-SS-B/La autoantibodies.
25860259	0.93	torsinB in the modulation of the effects of torsinA on dopamine receptor protein expression remains speculative.
	0.72	torsinB, which shares 70% homology with torsinA. We have shown previously that torsinA expression in the brain is high during development and low at maturity, whereas torsinB expression shows the opposite trend (low during development and high at maturity).
28198698	0.91	torsinB was knocked down in fibroblasts from a DYT1 mutant background, nuclear envelope defects were seen in non-neuronal cells as well, demonstrating that torsinB can compensate for loss of torsinA. To determine whether a similar compensation can occur in the CNS, Tanabe et al used embryoid bodies derived from DYT1 KI animals and showed that either torsinA or torsinB can individually rescue the abnormal nuclear envelope budding when the cells are differentiated into neural lineage.
22880064	0.66	torsinB, which is expressed in non-neuronal cells in vivo and the cells lines used for the above referenced experiments, is functionally redundant with torsinA. Finally, there is a fundamental difference between cell-based overexpression and this mouse model.
23893455	0.66	torsinA, torsinB, torsin2A, and torsin3A.
21305521	0.61	DQ1 trans-heterodimers are more stable than between DQA1*01 and beta chains of DQ2 and DQ3 which has been shown to be due to the steric incompatibility resulting from structural differences.