Complex formation and submembranous localization of annexin 2 and S100A10 in live HepG2 cells
2001; Wiley; Volume: 500; Issue: 3 Linguagem: Inglês
10.1016/s0014-5793(01)02604-7
ISSN1873-3468
AutoresNicole Zobiack, Volker Gerke, Ursula Rescher,
Tópico(s)Protease and Inhibitor Mechanisms
ResumoThe Ca 2+ and membrane binding protein annexin 2 can form a heterotetrameric complex with the S100A10 protein and this complex is thought to serve a bridging or scaffolding function in the membrane underlying cytoskeleton. To elucidate which of the subunits targets the complex to the subplasmalemmal region in live cells we employed YFP/CFP fusion proteins and live cell imaging in HepG2 cells. We show that monomeric annexin 2 is targeted to the plasma membrane whereas non‐complexed S100A10 acquires a general cytosolic distribution. Co‐expression of S100A10 together with annexin 2 and the resulting complex formation, however, lead to a recruitment of S100A10 to the plasma membrane thus identifying annexin 2 as the membrane targeting subunit.
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