A novel PKC-regulated mechanism controls CD44-ezrin association and directional cell motility

被引:200
作者
Legg, JW
Lewis, CA
Parsons, M
Ng, T
Isacke, CM
机构
[1] Inst Canc Res, Chester Beatty Labs, Breakthrough Toby Robins Breast Canc Res Ctr, London SW3 6JB, England
[2] Univ London Imperial Coll Sci Technol & Med, Dept Biol Sci, London SW7 2AZ, England
[3] St Thomas Hosp, Richard Dimbleby ICRF Dept Canc Res, London SE1 7EH, England
关键词
D O I
10.1038/ncb797
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The dynamic assembly and disassembly of membrane-cytoskeleton junctional complexes is critical in cell migration. Here we describe a novel phosphorylation mechanism that regulates the hyaluronan receptor CD44. In resting cells, CD44 is constitutively phosphorylated at a single serine residue, Ser325. After protein kinase C is activated, a switch in phosphorylation results in CD44 being phosphorylated solely at an alternative residue, Ser291. Using fluorescence resonance energy transfer (FRET) monitored by fluorescence lifetime imaging microscopy (FLIM) and chemotaxis assays we show that phosphorylation of Ser291 modulates the interaction between CD44 and the cytoskeletal linker protein ezrin in vivo, and that this phosphorylation is critical for CD44-dependent directional cell motility.
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收藏
页码:399 / 407
页数:9
相关论文
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