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Thus, we characterized here MOSPD2, a novel tethering component related to VAP proteins(VAP-A and VAP-B), bridging the endoplasmic reticulum with a variety of distinct organelles.
report on a novel mutation of p.Pro56His in VABP found in a Chinese familial amyotrophic lateral sclerosis pedigree and description of the clinical characteristics of the family.
the component proteins of the machinery, OSBP, VAP, SAC1, and PITPNB, are all essential host factors for AiV replication. Importantly, the machinery is directly recruited to the RNA replication sites through previously unknown interactions of VAP/OSBP/SAC1 with the AiV proteins and with ACBD3.
Lifelong elevation of neuronal VAPB slowed the decline of neurological impairment, delayed denervation of hindlimb muscles, and prolonged survival of spinal motor neurons.
Study showed that alpha-synuclein perturbs endoplasmic reticulum-mitochondria associations and that this involves disruption to the VAPB-PTPIP51 tethering proteins. Using a range of assays including immunoprecipitation, cellular glutathione S-transferase pull-down, proximity ligation and in vitro binding of recombinant proteins, study showed that alpha-synuclein is a direct binding partner for VAPB.
ACBD5-VAPB interaction regulates peroxisome-endoplasmic reticulum associations. Loss of PO-ER association perturbs PO membrane expansion and increases PO movement.
VAP-ACBD5-mediated contact between the endoplasmic reticulum and peroxisomes mediate organelle maintenance and lipid homeostasis.
Effects of the combined absence of VAPA and VAPB in human cells were studied; cells lacking VAP accumulate high levels of PI4P, actin comets, and trans-Golgi proteins on endosomes. Such defects are mimicked by downregulation of OSBP, a VAP interactor and PI4P transporter that participates in VAP-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 domain which overlaps with those for binding HCV NS5A and human Eph receptors.
The VAPB and its interacting partners cooperatively regulate protein trafficking through the ERGIC by modulating PtdIns4P levels.
Collectively, these results not only lead to a better understanding of hVAPB function but also point to potentially relevant targets for therapeutic intervention.
results suggest that the binding of vesicle-associated membrane protein-associated protein B(VAP-B) to Rab3 GTPase activating protein 1(RAB3GAP1) is implicated in the regulation of nuclear envelope formation through ER-Golgi intermediate compartment
P56S-VAPB was found to suppress adipocyte differentiation by promoting the activation of the ATF4-CHOP pathway
The repertoire of VAPB interactors is more diverse than previously anticipated and link VAPB to the function of ATPase complexes such as p97/FAF1 and ASNA1/transmembrane-domain recognition complex.
In patients with familial or sporadic amyotrophic lateral sclerosis (ALS) from Portugal, Iceland and Sweden no association is found with disease and VAMP-associated protein type B (VAPB) mutations.
Findings provide new pathophysiological mechanisms of P56S VAPB that differentially affect the function and survival of corticospinal and spinal motor neurons in familial amyotrophic lateral sclerosis 8.
There was colocalization of Kv2.1 and Kv2.2 with endogenous VAPB at ER-PM junctions in mouse brain neurons. Expression of Kv2.1 recruits VAPB to ER-PM junctions.The domains of VAPs and Kv2.1 necessary and sufficient for their association at ER-PM junctions were identified.
Peroxisomal (PO) long range movements were largely diminished in response to human ACBD5 overexpression in primary mouse hippocampal neurons. PO localization significantly changed in ACBD5-transfected neurons, PO numbers in neurites increased, while PO density in the soma was decreased. Alterations in PO motility and distribution in the hippocampal neurons were independent of the interaction between ACBD5 and mouse Vapb.
ignificant alterations of the vesicle-associated membrane protein-associated protein B (VAPB) and its downstream pathways such as mitochondrial calcium uptake and autophagy were detected in dominant GARS mutations. The role of VAPB has been supported by similar results in the GarsC210R mice. Our data suggest that altered mitochondria-associated endoplasmic reticulum (ER) membranes (MAM) may be important disease mechanisms
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-XBP1 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 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-mediated osteoclastogenesis via PLCgamma2-Ca(2+)-NFAT signaling
Co-expression of mutant protein-associated protein B (VAPB) enhances the transactive response DNA-binding protein-43 (TDP-43)-induced motor neuronal cell death while that of wild type-VAPB attenuates it.
Adeno-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 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.
VAMP-associated 33 kDa protein
, 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 protein B
, vesicle-associated membrane protein, associated protein B and C
, vesicle-associated membrane protein-associated protein B
, VAMP-associated protein 33b
, VAMP (vesicle-associated membrane protein)-associated protein B and C L homeolog