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.