Tyrosine 734 of NCAM180 interferes with FGF receptor-dependent signaling implicated in neurite growth

被引:14
作者
Diestel, S
Laurini, C
Traub, O
Schmitz, B
机构
[1] Inst Physiol Biochem & Anim Hlth, Dept Biochem, D-53115 Bonn, Germany
[2] Univ Bonn, Genet Inst, Dept Mol Biol, D-53117 Bonn, Germany
关键词
D O I
10.1016/j.bbrc.2004.07.100
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The cytoplasmic domain of the neural cell adhesion molecule (NCAM) contains multiple phosphorylation sites. We report here that in addition to serine and threonine residues a tyrosine of the NCAM180 isoform is phosphorylated as shown by phosphoamino acid analysis. Exchange of the only cytoplasmic tyrosine at position 734 of human NCAM180 (NCAM180-Y734F) to phenylalanine resulted in increased neurite outgrowth of NCAM180-Y734F transfected B35 neuroblastoma cells compared to NCAM180-wt transfectants on poly-L-lysine as substrate. As demonstrated by inhibitor studies the increased neurite outgrowth was due to higher FGF receptor 1 and ERK1 activity in NCAM180-Y734F cells, indicating that tyrosine residue 734 plays a role in signal transduction mediated by the FGF receptor. On an NCAM expressing monolayer of COS-7 cells the Y734F mutation also influences FGF receptor 1 dependent neurite outgrowth, but under these conditions additional mechanisms seem to be responsible for the increased neurite length observed for NCAM180-Y734F transfected cells. (C) 2004 Elsevier Inc. All rights reserved.
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收藏
页码:186 / 196
页数:11
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