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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 15 May 2015.

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, CAN, A-4, LAMP-2
Papers on Vma21p
Muscle MRI abnormalities in X-linked myopathy with excessive autophagy.
New
Péréon et al., Nantes, France. In Muscle Nerve, 25 Apr 2015
INTRODUCTION: X-linked myopathy with excessive autophagy (XMEA) is an X-linked recessive myopathy due to recently reported mutations in the VMA21 gene.
No cardiomyopathy in X-linked myopathy with excessive autophagy.
New
Minassian et al., Turku, Finland. In Neuromuscul Disord, 17 Apr 2015
XMEA is caused by compromised acidification of lysosomes resulting from hypofunction of the proton pump vacuolar ATPase (V-ATPase), due to hypomorphic mutations in VMA21, whose protein product assembles V-ATPase.
Non-coding VMA21 deletions cause X-linked myopathy with excessive autophagy.
New
Minassian et al., Milano, Italy. In Neuromuscul Disord, Mar 2015
All XMEA mutations to date have been single-nucleotide substitutions that reduce VMA21 expression, which leads to modest lysosomal pH increase, the first step in the disease's pathogenesis.
Autophagic vacuolar pathology in desminopathies.
New
Harms et al., Saint Louis, United States. In Neuromuscul Disord, Mar 2015
These features have been most clearly described in patients with Danon's disease due to LAMP2 deficiency and X-linked myopathy with excessive autophagy (XMEA) due to mutations in VMA21.
X-linked myopathy with excessive autophagy: a failure of self-eating.
New
Minassian et al., Toronto, Canada. In Acta Neuropathol, Mar 2015
Mutations in the VMA21 gene at Xq28 cause XMEA by reducing the activity of lysosomal hydrolases.
Tubulin- and actin-associating GIMAP4 is required for IFN-γ secretion during Th cell differentiation.
New
Henttinen et al., Turku, Finland. In Immunol Cell Biol, Feb 2015
We demonstrate that depletion of GIMAP4 with RNAi results in downregulation of endoplasmic reticulum localizing chaperone VMA21.
Late adult-onset of X-linked myopathy with excessive autophagy.
New
Moore et al., Iowa City, United States. In Muscle Nerve, Jul 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.
Matsumoto et al., Hiroshima, Japan. In Neuromuscul Disord, 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.
Minassian et al., Toronto, Canada. In Acta Neuropathol, 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.
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.
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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