The actin cross-linking protein AFAP120 regulates axon elongation in a tyrosine phosphorylation-dependent manner

NEUROSCIENCE LETTERS

卷:444

Article

Harder, Jennifer¹  Xu, Xiaohua¹  Letourneau, Paul¹  Lanier, Lorene M.¹ 

[1] Univ Minnesota, Dept Neurosci, Minneapolis, MN 55455 USA

关键词: Axon elongation;    Growth cone;    Src kinase;    Actin cytoskeleton;    AFAP;   

DOI  :  10.1016/j.neulet.2008.08.036

来源: Elsevier

【 摘 要 】

Growth cone guidance and axon elongation require the dynamic coordinated regulation of the actin cytoskeleton. As the growth cone moves, actin-dependent forces generate tension that enables protrusive activity in the periphery and drives growth cone translocation. This dynamic remodeling of the actin cytoskeleton in response to membrane tension requires activation of Src kinase. Although it has been proposed that these actin-dependent forces vary with the extent of actin cross-linking, the identity of the cross-linking protein(s) remains unknown. AFAP120 is a nervous system specific actin cross-linking protein that is regulated by Src kinase phosphorylation. Here, we report that AFAP120 is expressed and tyrosine phosphorylated in differentiating cerebellar granule cells, where it is enriched in the axon and growth cone. Over-expression of AFAP120 enhances neurite elongation in a tyrosine phosphorylation-dependent manner. These findings suggest that AFAP120 may coordinate Src signaling with the dynamic changes in the actin cytoskeleton that drive growth cone motility and axon elongation. (C) 2008 Elsevier Ireland Ltd. All rights reserved.

【 授权许可】

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