No cardiomyopathy in X-linked myopathy with excessive autophagy.
Turku, Finland. In Neuromuscul Disord, 30 Jun 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.
Autophagic vacuolar pathology in desminopathies.
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.
Role of Vma21p in assembly and transport of the yeast vacuolar ATPase.
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.
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.
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.
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.