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Study showed that alpha-synuclein perturbs endoplasmic reticulum-mitochondria associations and that this involves disruption to the VAPB-PTPIP51 (show FAM82A2 ELISA Kits) tethering proteins. Using a range of assays including immunoprecipitation, cellular glutathione S-transferase (show GSTa2 ELISA Kits) pull-down, proximity ligation and in vitro binding of recombinant proteins, study showed that alpha-synuclein is a direct binding partner for VAPB.
ACBD5 (show ACBD5 ELISA Kits)-VAPB interaction regulates peroxisome-endoplasmic reticulum associations. Loss of PO-ER association perturbs PO membrane expansion and increases PO movement.
VAP (show F10 ELISA Kits)-ACBD5 (show ACBD5 ELISA Kits)-mediated contact between the endoplasmic reticulum and peroxisomes mediate organelle maintenance and lipid homeostasis.
Effects of the combined absence of VAPA (show VAPA ELISA Kits) and VAPB in human cells were studied; cells lacking VAP (show F10 ELISA Kits) accumulate high levels of PI4P, actin comets, and trans-Golgi proteins on endosomes. Such defects are mimicked by downregulation of OSBP (show OSBP ELISA Kits), a VAP (show F10 ELISA Kits) interactor and PI4P transporter that participates in VAP (show F10 ELISA Kits)-dependent endoplasmic reticulum-endosomes tethers.
this is the first study to report Amyotrophic lateral sclerosis caused by a VAPB mutation in a Chinese population.
Our work revealed that VAP-A/B knockdown impaired the processing and secretion of PAUF, which is one of the cargo proteins of carriers of the trans-Golgi network to the cell surface.
Heterozygous P56S Vapb knock-in mice show mild age-dependent defects in motor behaviors as characteristic features of the disease. The homozygous P56S Vapb knock-in mice show more severe defects compared with heterozygous mice reflecting the dominant and dose-dependent effects of P56S mutation.
VAPB inhibited the degradation of DeltaF508-CFTR in the ER through interactions with the RMA1-Derlin-BAP31-VCP pathway.
Study characterizes the human VAPB-HCV NS5B interaction and reveals that NS5B C-linker is intrinsically disordered in solution but capable of binding the human VAPB-MSP (show MSMB ELISA Kits) domain which overlaps with those for binding HCV NS5A and human Eph (show EPHA1 ELISA Kits) receptors.
The VAPB and its interacting partners cooperatively regulate protein trafficking through the ERGIC by modulating PtdIns4P levels.
To identify pathological defects in animals expressing the P56S mutant VAPB protein at physiological levels in the appropriate tissues, we have generated Vapb knock-in mice
The disruption of the IRE1 (show ERN1 ELISA Kits)-XBP1 (show XBP1 ELISA Kits) pathway is a cause for the reduced myotube formation in P56S-VAPB-mutation expressing cells.
Vapb knock-out mice exhibit abnormal muscular triacylglycerol levels and FoxO (show FOXO3 ELISA Kits) target gene transcriptional responses to fasting and refeeding
Mice knocked-out for Vapb showed mild motor deficits after 18 months of age.
VapB positively regulates RANKL (show TNFSF11 ELISA Kits)-mediated osteoclastogenesis via PLCgamma2 (show PLCG2 ELISA Kits)-Ca(2 (show CA2 ELISA Kits)+)-NFAT (show NFATC1 ELISA Kits) signaling
Co-expression of mutant protein-associated protein B (show LEPREL2 ELISA Kits) (VAPB) enhances the transactive response DNA-binding protein (show HSF4 ELISA Kits)-43 (TDP-43 (show TARDBP ELISA Kits))-induced motor neuronal cell death while that of wild type-VAPB attenuates it.
Adeno (show ADORA2A ELISA Kits)-associated viral-mediated over-expression of both wild-type and mutated form of human VAPB selectively induces death of primary motor neurons, albeit with different kinetics.
However, VAPBP56S but not VAPBwt transgenic mice develop cytoplasmic TDP-43 (show TARDBP ELISA Kits) accumulations within spinal cord motor neurons that were first detected at 18 months of age.
The total loss of VAPB function in unfolded protein response, induced by one P56S mutant allele, may contribute to the development of P56SVAPB- induced amyotrophic lateral sclerosis.
The protein encoded by this gene is a type IV membrane protein found in plasma and intracellular vesicle membranes. The encoded protein is found as a homodimer and as a heterodimer with VAPA. This protein also can interact with VAMP1 and VAMP2 and may be involved in vesicle trafficking.
vesicle-associated membrane protein-associated protein B/C
, VAMP (vesicle-associated membrane protein)-associated protein B and C
, VAMP-associated protein B/C
, VAMP-associated 33 kDa protein
, VAMP-associated protein B
, vesicle-associated membrane protein-associated protein B
, vesicle-associated membrane protein, associated protein B and C
, VAMP-associated protein 33b