Evidence for a pool of coronin in mammalian cells that is sensitive to PI 3‐kinase

FEBS Letters

Thelen, M.²  Didichenko, S.A.²  Segal, A.W.¹ 

[1] Department of Medicine, University College London, 5 University Street, London WC1E 6JJ, UK;Institute of Research in Biomedicine, Via Vela 6, CH-6501 Bellinzona, Switzerland

关键词: Coronin;    Phosphatidylinositol 3-kinase;    Phagocytosis;    Macrophage;   

DOI  :  10.1016/S0014-5793(00)02220-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown