| CALCOCO1 acts with VAMP-associated proteins to mediate ER-phagy. | CALCOCO1 acts with VAMP-associated proteins to mediate ER-phagy.
Nthiga TM, Kumar Shrestha B, Sjøttem E, Bruun JA, Bowitz Larsen K, Bhujabal Z, Lamark T, Johansen T., Free PMC Article | 04/13/2021 |
| Proteomics-Based Approach Identifies Altered ER Domain Properties by ALS-Linked VAPB Mutation. | Proteomics-Based Approach Identifies Altered ER Domain Properties by ALS-Linked VAPB Mutation.
Yamanaka T, Nishiyama R, Shimogori T, Nukina N., Free PMC Article | 12/5/2020 |
| 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. | Identification of VAPA and VAPB as Kv2 Channel-Interacting Proteins Defining Endoplasmic Reticulum-Plasma Membrane Junctions in Mammalian Brain Neurons.
Kirmiz M, Vierra NC, Palacio S, Trimmer JS., Free PMC Article | 10/19/2019 |
| 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. | Intracellular redistribution of neuronal peroxisomes in response to ACBD5 expression.
Wang Y, Metz J, Costello JL, Passmore J, Schrader M, Schultz C, Islinger M., Free PMC Article | 06/1/2019 |
| 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 | Mutations in glycyl-tRNA synthetase impair mitochondrial metabolism in neurons.
Boczonadi V, Meyer K, Gonczarowska-Jorge H, Griffin H, Roos A, Bartsakoulia M, Bansagi B, Ricci G, Palinkas F, Zahedi RP, Bruni F, Kaspar B, Lochmüller H, Boycott KM, Müller JS, Horvath R., Free PMC Article | 03/2/2019 |
| 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 | Vapb/Amyotrophic lateral sclerosis 8 knock-in mice display slowly progressive motor behavior defects accompanying ER stress and autophagic response.
Larroquette F, Seto L, Gaub PL, Kamal B, Wallis D, Larivière R, Vallée J, Robitaille R, Tsuda H., Free PMC Article | 09/17/2016 |
| The disruption of the IRE1-XBP1 pathway is a cause for the reduced myotube formation in P56S-VAPB-mutation expressing cells. | ALS-Linked P56S-VAPB Mutation Impairs the Formation of Multinuclear Myotube in C2C12 Cells.
Tokutake Y, Yamada K, Ohata M, Obayashi Y, Tsuchiya M, Yonekura S., Free PMC Article | 05/14/2016 |
| Vapb knock-out mice exhibit abnormal muscular triacylglycerol levels and FoxO target gene transcriptional responses to fasting and refeeding | VAPB/ALS8 MSP ligands regulate striated muscle energy metabolism critical for adult survival in caenorhabditis elegans.
Han SM, El Oussini H, Scekic-Zahirovic J, Vibbert J, Cottee P, Prasain JK, Bellen HJ, Dupuis L, Miller MA., Free PMC Article | 03/22/2014 |
| Mice knocked-out for Vapb showed mild motor deficits after 18 months of age. | Investigating the contribution of VAPB/ALS8 loss of function in amyotrophic lateral sclerosis.
Kabashi E, El Oussini H, Bercier V, Gros-Louis F, Valdmanis PN, McDearmid J, Mejier IA, Dion PA, Dupre N, Hollinger D, Sinniger J, Dirrig-Grosch S, Camu W, Meininger V, Loeffler JP, René F, Drapeau P, Rouleau GA, Dupuis L. | 01/4/2014 |
| VapB positively regulates RANKL-mediated osteoclastogenesis via PLCgamma2-Ca(2+)-NFAT signaling | VapB as a regulator of osteoclastogenesis via modulation of PLCγ2-Ca(2+)-NFAT signaling.
Choi SW, Yeon JT, Park KI, Lee CH, Youn BS, Oh J, Lee MS. | 03/17/2012 |
| 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. | Amyotrophic lateral sclerosis-linked mutant VAPB enhances TDP-43-induced motor neuronal toxicity.
Suzuki H, Matsuoka M. | 01/14/2012 |
| 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. | AAV-mediated expression of wild-type and ALS-linked mutant VAPB selectively triggers death of motoneurons through a Ca2+-dependent ER-associated pathway.
Langou K, Moumen A, Pellegrino C, Aebischer J, Medina I, Aebischer P, Raoul C. | 10/23/2010 |
| 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. | Amyotrophic lateral sclerosis mutant vesicle-associated membrane protein-associated protein-B transgenic mice develop TAR-DNA-binding protein-43 pathology.
Tudor EL, Galtrey CM, Perkinton MS, Lau KF, De Vos KJ, Mitchell JC, Ackerley S, Hortobágyi T, Vámos E, Leigh PN, Klasen C, McLoughlin DM, Shaw CE, Miller CC. | 07/5/2010 |
| 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. | ALS-linked P56S-VAPB, an aggregated loss-of-function mutant of VAPB, predisposes motor neurons to ER stress-related death by inducing aggregation of co-expressed wild-type VAPB.
Suzuki H, Kanekura K, Levine TP, Kohno K, Olkkonen VM, Aiso S, Matsuoka M. | 01/21/2010 |