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@ARTICLE{Shaikh:1047310,
author = {Shaikh, Imran G. and Kostritskii, Andrei Y. and Renigunta,
Aparna and Jeschke, Julia and Halaszovich, Christian R. and
Zhao, Wencai and Geissler, Marc and Bhushan, Sudhanshu and
Weber, Stefanie and Meinhardt, Andreas and Machtens,
Jan-Philipp and Oliver, Dominik and Renigunta, Vijay},
title = {{E}lectrochemical coupling at the plasma membrane by mouse
voltage-sensitive phosphatase requires association with
basigin},
journal = {Cell reports},
volume = {44},
number = {9},
issn = {2211-1247},
address = {Maryland Heights, MO},
publisher = {Cell Press},
reportid = {FZJ-2025-04225},
pages = {116200 -},
year = {2025},
note = {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.},
abstract = {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.},
cin = {IBI-1},
ddc = {610},
cid = {I:(DE-Juel1)IBI-1-20200312},
pnm = {5241 - Molecular Information Processing in Cellular Systems
(POF4-524) / DFG project G:(GEPRIS)426950122 - FOR 5046:
Integrative Analyse epithelialer SLC26 Anionentransporter
– von der molekularen Struktur zur Pathophysiologie
(426950122)},
pid = {G:(DE-HGF)POF4-5241 / G:(GEPRIS)426950122},
typ = {PUB:(DE-HGF)16},
pubmed = {40880230},
UT = {WOS:001564218300001},
doi = {10.1016/j.celrep.2025.116200},
url = {https://juser.fz-juelich.de/record/1047310},
}