TY  - JOUR
AU  - Shaikh, Imran G.
AU  - Kostritskii, Andrei Y.
AU  - Renigunta, Aparna
AU  - Jeschke, Julia
AU  - Halaszovich, Christian R.
AU  - Zhao, Wencai
AU  - Geissler, Marc
AU  - Bhushan, Sudhanshu
AU  - Weber, Stefanie
AU  - Meinhardt, Andreas
AU  - Machtens, Jan-Philipp
AU  - Oliver, Dominik
AU  - Renigunta, Vijay
TI  - Electrochemical coupling at the plasma membrane by mouse voltage-sensitive phosphatase requires association with basigin
JO  - Cell reports
VL  - 44
IS  - 9
SN  - 2211-1247
CY  - Maryland Heights, MO
PB  - Cell Press
M1  - FZJ-2025-04225
SP  - 116200 -
PY  - 2025
N1  - We thank Olga Ebers, Galina Zielke, and Nesli Oezen for excellent technical assistance.We gratefully acknowledge the gifts of mVSP from S.M. Bajjalieh, Ci-VSPand Dr-VSP from Y. Okamura, Xl-VSP from W. Ratzan, NPTN ERret from B. Fakler,PLCδ1-PH from T. Balla, Lyn11 from T. Meyer, tubby-Cterm from L. Shapiro, andTAPP1-PH from D. Alessi. This work was supported by grants from the von Behring-Ro¨ ntgen-Stiftung (65-0028) to D.O., V.R., A.M., and S.B.; from the DeutscheForschungsgemeinschaft (DFG; German Research Foundation) to V.R. (RE 4617/2-1), D.O. (OL 240/8-1 as part of the Research Unit FOR 5046, project P3), andJ.-P.M. (MA 7525/2-2, as part of the Research Unit FOR 5046, project P2); andby the LOEWE Research Focus CoroPan (Project P5), funded by the State ofHesse, Germany (to V.R. and A.R.) The authors gratefully acknowledge thecomputing time granted through JARA on the supercomputer JURECA at ForschungszentrumJu¨ lich under grant mpogt.
AB  - Voltage-sensitive phosphatases (VSPs) are unique enzymes that mediate electrochemical coupling by convertingphosphoinositides in response to membrane depolarization. In mammals, VSPs are involved in regulatingsperm motility. The basic functionality of mammalian VSPs has remained enigmatic, as retention tointracellular compartments precluded functional analysis. Here, a membrane yeast two-hybrid assay identifiesbasigin as an accessory subunit of mouse VSP (mVSP). Co-expression with basigin or its homologsinduced trafficking of mVSP from the endoplasmic reticulum to the plasma membrane. Mutational analysisand structural predictions by AlphaFold-Multimer showed that the functional effect on mVSP requires interactionof the transmembrane region of basigin with the voltage sensor domain of mVSP. Basigin-mediatedsurface localization allowed for functional analysis, revealing that mVSP acts as a voltage-activated5-phosphatase against PI(4,5)P 2 and PI(3,4,5)P 3 with a more negative activation range compared to nonmammalianVSPs.
LB  - PUB:(DE-HGF)16
C6  - 40880230
UR  - <Go to ISI:>//WOS:001564218300001
DO  - DOI:10.1016/j.celrep.2025.116200
UR  - https://juser.fz-juelich.de/record/1047310
ER  -