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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 18 Mar 2014.

VMA21 Vma21p

Vma21p, XMEA, VMA21
This gene encodes a chaperone for assembly of lysosomal vacuolar ATPase.[provided by RefSeq, Jul 2012] (from NCBI)
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Top mentioned proteins: ATPase, V-ATPase, A-4, CAN, HAD
Papers on Vma21p
Late-adult onset of X-linked myopathy with excessive autophagy (XMEA).
New
Moore et al., Iowa City, United States. In Muscle Nerve, 01 Mar 2014
Conclusions: This case expands the clinical phenotype of XMEA and suggests VMA21 sequencing be considered in evaluating men with LAMP2-positive autophagic vacuolar myopathy.
Elevated urinary β2 microglobulin in the first identified Japanese family afflicted by X-linked myopathy with excessive autophagy.
New
Matsumoto et al., Hiroshima, Japan. In Neuromuscul Disord, Nov 2013
High urinary β2 microglobulin, normal serum β2 microglobulin, autophagic vacuoles with sarcolemmal features, and a hemizygous c.164-7T>G mutation in the VMA21 gene were found.
VMA21 deficiency prevents vacuolar ATPase assembly and causes autophagic vacuolar myopathy.
New
Minassian et al., Toronto, Canada. In Acta Neuropathol, Mar 2013
We show that XMEA is caused by hypomorphic alleles of the VMA21 gene, that VMA21 is the diverged human ortholog of the yeast Vma21p protein, and that like Vma21p, VMA21 is an essential assembly chaperone of the vacuolar ATPase (V-ATPase), the principal mammalian proton pump complex.
A genome-wide enhancer screen implicates sphingolipid composition in vacuolar ATPase function in Saccharomyces cerevisiae.
Stevens et al., Eugene, United States. In Genetics, 2011
To identify additional elements that affect V-ATPase assembly, trafficking, or enzyme activity, we performed a genome-wide enhancer screen in the budding yeast Saccharomyces cerevisiae with two mutant assembly factor alleles, VMA21 with a dysfunctional ER retrieval motif (vma21QQ) and vma21QQ in combination with voa1Δ, a nonessential assembly factor.
Impaired autophagy in sporadic inclusion-body myositis and in endoplasmic reticulum stress-provoked cultured human muscle fibers.
Askanas et al., Los Angeles, United States. In Am J Pathol, 2010
Moreover, in cultured human muscle fibers, ERS induction significantly decreased activities of cathepsins D and B, increased levels of LC3-II, decreased phosphorylation of p70S6 kinase, and decreased expression of VMA21, a chaperone for assembly of lysosomal V-ATPase.
[Eludication of pathomechanism of and development of therapy for autophagic vacuolar myopathies].
Nishino, In Rinsho Shinkeigaku, 2010
Other AVSF myopathies include X-linked myopathy with excessive autophagy which is now known to be caused by VMA21 mutations.
VMA21 deficiency causes an autophagic myopathy by compromising V-ATPase activity and lysosomal acidification.
Impact
Minassian et al., Toronto, Canada. In Cell, 2009
We show that XMEA is caused by hypomorphic alleles of the VMA21 gene, that VMA21 is the diverged human ortholog of the yeast Vma21p protein, and that like Vma21p it is an essential assembly chaperone of the V-ATPase, the principal mammalian proton pump complex.
VMA21 deficiency: a case of myocyte indigestion.
Impact
DiMauro et al., New York City, United States. In Cell, 2009
The Vma21p protein in yeast is an essential assembly chaperone for the vacuolar ATPase, the major proton pump of cellular membranes.
Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum.
Stevens et al., Eugene, United States. In Mol Biol Cell, 2008
The role of Voa1p in V(0) assembly was revealed in cells expressing an ER retrieval-deficient form of the V-ATPase assembly factor Vma21p (Vma21pQQ).
Arabidopsis has two functional orthologs of the yeast V-ATPase assembly factor Vma21p.
Schumacher et al., Tübingen, Germany. In Traffic, 2008
We show in this study that two ER-localized Arabidopsis proteins that share only 25% sequence identity with Vma21p can functionally replace this yeast assembly factor.
Genetic and molecular interactions of the Erv41p-Erv46p complex involved in transport between the endoplasmic reticulum and Golgi complex.
Otte et al., Chicago, United States. In J Cell Sci, 2006
We identified synthetic interactions with vma12, vma21, vma22 and vps1 deletion mutations.
PKR1 encodes an assembly factor for the yeast V-type ATPase.
Graham et al., Salt Lake City, United States. In J Biol Chem, 2006
Finally, overexpression of the V-ATPase assembly factor Vma21p suppresses the growth and acidification defects of pkr1Delta cells.
Role of Vma21p in assembly and transport of the yeast vacuolar ATPase.
GeneRIF
Schekman et al., Berkeley, United States. In Mol Biol Cell, 2004
Vma21p is not involved in regulating the interaction between V0 and V1 sectors of vacuolar ATPase, but it has a crucial role in coordinating the assembly of V0 subunits and in escorting the assembled V0 complex into ER-derived transport vesicles
Structure and assembly of the yeast V-ATPase.
Review
Stevens et al., Eugene, United States. In J Bioenerg Biomembr, 2003
Homologues of the Vma21p assembly factor have been identified in many higher eukaryotes supporting a ubiquitous assembly pathway for this important enzyme complex.
Composition and assembly of the yeast vacuolar H(+)-ATPase complex.
Review
Stevens et al., Eugene, United States. In J Exp Biol, 2000
The assembly factors designated Vma12p, Vma21p and Vma22p have been localized to the membrane of the endoplasmic reticulum and aid the association of newly synthesized V-ATPase subunits translocated into the endoplasmic reticulum membrane.
Assembly of the yeast vacuolar proton-translocating ATPase.
Review
Stevens et al., Eugene, United States. In J Bioenerg Biomembr, 1999
The assembly factors, Vma12p, Vma21p, and Vma22p are localized to the endoplasmic reticulum (ER) and aid the assembly of newly synthesized V-ATPase subunits that are translocated into the ER membrane.
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