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Evidence for a pool of coronin in mammalian cells that is sensitive to PI 3‐kinase
Author(s) -
Didichenko S.A.,
Segal A.W.,
Thelen M.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02220-1
Subject(s) - wortmannin , pi , microbiology and biotechnology , phosphatidylinositol , biology , kinase , phagocytosis , phagosome , cytoskeleton , protein kinase c , actin , protein kinase a , biochemistry , cell
Coronin, a 57 kDa actin binding protein elutes with an apparent molecular mass of 400–600 kDa from gel filtration columns. This fraction is not unrelated to the reported 200 kDa complex where coronin is associated with phox proteins of the NADPH‐oxidase. Phosphatidylinositol 3‐kinase (PI 3‐kinase) solubilizes coronin from the 400–600 kDa complex, thus constitutive active PI 3‐kinase is sufficient to disrupt the complex, whereas wortmannin stabilizes it. Conversely, the phox protein associated pool of coronin is PI 3‐kinase independent. During phagocytosis coronin is recruited together with PI 3‐kinase to membranes of nascent and early phagosomes co‐localizing with the actin cytoskeleton, confirming that coronin contributes to phagocytosis.