Lateral mobility of FcγRIIa is reduced by protein kinase C activation

FEBS Letters

Odin, Joseph A.¹  Zhang, Fen²  Shen, Zhenhai¹  Yang, Bing²  Lin, Ching-Tai¹  Unkeless, Jay C.¹  Jacobson, Ken² 

[1] Department of Biochemistry, Mount Sinai Medical Center, New York, NY 10029, USA;Department of Cell Biology and Anatomy, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7090, USA

关键词: Fc receptor;    Protein kinase C;    Fluorescence recovery after photobleaching;    Lateral mobility;    FRAP;    fluorescence recovery after photobleaching;    PKC;    protein kinase C;    PBS(+);    phosphate-buffered saline with Ca2+ and Mg2+;    PMA;    phorbol myristate acetate;    FcγR;    receptor for the Fc domain of immunoglobulin G;    wt;    wild type;   

DOI  :  10.1016/0014-5793(95)01249-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The lateral mobility of membrane proteins can reflect the extent of various protein-protein interactions. Using the fluorescence recovery after photobleaching technique, we have studied the lateral mobility of human FcγRIIa and some FcγRIIa mutants expressed in either P388D1 cells, a mouse macrophagelike cell line, or in Chinese hamster ovary (CHO) cells [1]. After treatment with phorbol myristate acetate (PMA), only the FcγRIIa molecules capable of mediating rapid endocytosis of immune complexes exhibited a reduced lateral diffusion coefficient with respect to untreated controls. Wild type FcγRIIa expressed in CHO cells, and nonfunctional FcγRIIa mutants expressed in P388D1 cells did not show any differences upon PMA treatment. This finding suggests that protein kinase C activation evokes additional protein-protein interactions with the cytoplasmic domain of functional FcγRIIa, which reduced receptor lateral mobility. The identity of these putative interacting proteins and the nature of the interactions remain to be elucidated.

【 授权许可】

Unknown