Article
Inhibitors of V-ATPase proton transport reveal uncoupling functions of tether linking cytosolic and membrane domains of V0 subunit a (Vph1p).
The Journal of biological chemistry - 23 Mar 2012
Chan Chun-Yuan, Prudom Catherine, Raines Summer M, Charkhzarrin Sahba, Melman Sandra D, De Haro Leyma P, Allen Chris, Lee Samuel A, Sklar Larry A, Parra Karlett J
Abstract excerpt
Vacuolar ATPases (V-ATPases) are important for many cellular processes, as they regulate pH by pumping cytosolic protons into intracellular organelles. The cytoplasm is acidified when V-ATPase is inhibited; thus we conducted a high-throughput screen of a chemical library to search for compounds that acidify the yeast cytosol in vivo using pHluorin-based flow cytometry. Two inhibitors, alexidine dihydrochloride...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.