VMA4 Antibody

1. Glu-44 is one of the key functional residues for subunit interaction in the V-ATPase complex. PMID: 24196958
2. Data indicate the interactions in V-ATPase Vma4 (subunit E) and Vma10 (subunit G). PMID: 23071676
3. new structural details of subunit E are discussed in the light of the structural arrangements of this subunit inside the V- and VV ATPase. PMID: 21826517
4. NMR solution structure of subunit E (fragment E(1-69)) of the Saccharomyces cerevisiae V (1)V (O) ATPase. PMID: 21399923
5. Mutational analysis of V-ATPase indicates that subunit E could communicate cellular changes to the catalytic sites upon binding to regulatory proteins which interact with subunit E as a means of regulating V-ATPase function. PMID: 15718227
6. Protein interaction studies show that the N-terminal region of Vma4 (subunit E) is a key factor not only in the stator structure of the vacuolar ATPase rotary molecular motor, but also in mediating interactions with putative regulatory subunits. PMID: 15751969
7. an increase in the level of the TIM23 translocase associated with the cytochrome bc1-COX supercomplex is observed in the absence of Su e and Su g PMID: 18187422
8. These results suggest that subunit E, especially its amino-terminal domain, plays a pertinent role in the assembly of V-ATPase subunits in vacuolar membranes from mice and yeast. PMID: 18662668

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KEGG: sce:YOR332W

STRING: 4932.YOR332W