Can GAP-43 interact with brain spectrin?

被引:21
作者
Riederer, BM
Routtenberg, A
机构
[1] Univ Lausanne, Fac Med, Inst Biol Cellulaire & Morphol, CH-1005 Lausanne, Switzerland
[2] Northwestern Univ, Dept Psychol, Cresap Neurosci Lab, Evanston, IL 60208 USA
[3] Northwestern Univ, Dept Neurobiol, Cresap Neurosci Lab, Evanston, IL 60208 USA
来源
MOLECULAR BRAIN RESEARCH | 1999年 / 71卷 / 02期
基金
美国国家科学基金会;
关键词
blot overlay; brain spectrin; cytoskeleton; GAP-43; microtubule; rat; sedimentation assay; SpII Sigma 1;
D O I
10.1016/S0169-328X(99)00179-5
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
The growth-associated and presynaptic protein GAP-43 is important for axonal growth during brain development, for synaptic plasticity and in axonal regeneration [Benowitz, Routtenberg, TINS 12 (1987) 527]. It has been speculated that such growth may be mediated by cytoskeletal proteins. However, the interaction of GAP-43 with proteins of the presynaptic terminals is poorly characterized. Here, we analyze GAP-43 binding to cytoskeletal proteins by two different biochemical assays, by blot overlay and sedimentation. We find that immobilized brain spectrin (BS) is able to bind GAP-43. In contrast, little binding was observed to microtubule proteins and other elements of the cytoskeleton. Since GAP-43 is located presynaptically, it may bind to the presynaptic form. of BS (SpII Sigma 1). It is attractive to think that such an interaction would participate in the structural plasticity observed in growth cones and adult synapses. (C) 1999 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:345 / 348
页数:4
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