RRC ID 63154
Author Matsumoto N, Sekiya M, Fujimoto Y, Haga S, Sun-Wada GH, Wada Y, Nakanishi-Matsui M.
Title Functional complementation of V-ATPase a subunit isoforms in osteoclasts.
Journal J Biochem
Abstract In osteoclasts, the a3 isoform of the proton-pumping V-ATPase plays essential roles in anterograde trafficking of secretory lysosomes and extracellular acidification required for bone resorption. This study examined functional complementation of the a isoforms by exogenously expressing the a1, a2, and a3 isoforms in a3-knockout (KO) osteoclasts. The expression levels of a1 and a2 in a3KO osteoclasts were similar, but lower than that of a3. a1 significantly localized to lysosomes, whereas a2 slightly did. On the other hand, a2 interacted with Rab7, a regulator of secretory lysosome trafficking in osteoclasts, more efficiently than a1. a1 partly complemented the functions of a3 in secretory lysosome trafficking and calcium phosphate resorption, while a2 partly complemented the former but not the latter function.
Volume 169(4)
Pages 459-466
Published 2021-4-29
DOI 10.1093/jb/mvaa118
PII 5949122
PMID 33135054
MeSH Animals Isoenzymes / metabolism Lysosomes / enzymology* Lysosomes / genetics Mice Mice, Knockout Osteoclasts / enzymology* Protein Subunits* Vacuolar Proton-Translocating ATPases / genetics Vacuolar Proton-Translocating ATPases / metabolism* rab GTP-Binding Proteins / genetics rab GTP-Binding Proteins / metabolism rab7 GTP-Binding Proteins
IF 2.476
Human and Animal Cells 293T(RCB2202)