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Tubulin and CRMP‐2 complex is transported via Kinesin‐1
Author(s) -
Kimura Arimura Fukata Toshihide, Nariko, Yuko,
Watanabe Hiroyasu,
Iwamatsu Akihiro,
Kaibuchi Kozo
Publication year - 2005
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2005.03063.x
Subject(s) - kinesin , tubulin , microtubule , microbiology and biotechnology , axon , motor protein , microtubule associated protein , tetratricopeptide , chemistry , microtubule nucleation , biology , biochemistry , centrosome , gene , cell cycle
The transport of tubulin and microtubules in a growing axon is essential for axonal growth and maintenance. However, the molecular mechanism underlying the linkage of tubulin and microtubules to motor proteins is not yet clear. Collapsin response mediator protein‐2 (CRMP‐2) is enriched at the distal part of growing axons in primary hippocampal neurons and plays a critical role in axon differentiation through its interaction with tubulin dimer and Numb. In this study, we show that CRMP‐2 regulates tubulin transport by linking tubulin and Kinesin‐1. The C‐terminal region of CRMP‐2 directly binds to the tetratricopeptide repeat domain of kinesin light chain 1 (KLC1). Soluble tubulin binds to the middle of CRMP‐2 and forms a trimeric complex with CRMP‐2/KLC1. Furthermore, the movement of GFP–tubulin in the photobleached area is weakened by knockdown of KLCs or CRMP‐2. These results indicate that the CRMP‐2/Kinesin‐1 complex regulates soluble tubulin transport to the distal part of the growing axon.