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Calcium-stimulated disassembly of focal adhesions mediated by an ORP3/IQSec1 complex

Ryan S. D’Souza, Jun Yeul Lim, Alper Turgut, Kelly A. Servage, Junmei Zhang, Kim Orth, Nisha G. Sosale, Matthew J. Lazzara, Jeremy C. Allegood, James E. Casanova

2020eLife81 citationsDOIOpen Access PDF

Abstract

Coordinated assembly and disassembly of integrin-mediated focal adhesions (FAs) is essential for cell migration. Many studies have shown that FA disassembly requires Ca2+ influx, however our understanding of this process remains incomplete. Here, we show that Ca2+ influx via STIM1/Orai1 calcium channels, which cluster near FAs, leads to activation of the GTPase Arf5 via the Ca2+-activated GEF IQSec1, and that both IQSec1 and Arf5 activation are essential for adhesion disassembly. We further show that IQSec1 forms a complex with the lipid transfer protein ORP3, and that Ca2+ influx triggers PKC-dependent translocation of this complex to ER/plasma membrane (PM) contact sites adjacent to FAs. In addition to allosterically activating IQSec1, ORP3 also extracts PI4P from the PM, in exchange for phosphatidylcholine. ORP3-mediated lipid exchange is also important for FA turnover. Together, these findings identify a new pathway that links calcium influx to FA turnover during cell migration.

Topics & Concepts

Cell biologyORAI1Focal adhesionIntegrinChemistrySTIM1CalciumGTPaseCalcium signalingSmall GTPaseMotilityBiologyEndoplasmic reticulumBiochemistrySignal transductionCellOrganic chemistryIon Channels and ReceptorsConnexins and lens biologyNeurobiology and Insect Physiology Research
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