期刊
EMBO JOURNAL
卷 21, 期 3, 页码 281-293出版社
WILEY
DOI: 10.1093/emboj/21.3.281
关键词
fast axonal transport; glycogen synthase kinase 3; GSK-3; kinesin; microtubule
资金
- NIA NIH HHS [AG12646] Funding Source: Medline
- NINDS NIH HHS [R01 NS023320, NS23320, R01 NS023868, R01 NS041170, NS23868, R56 NS023868, NS41170] Funding Source: Medline
Membrane-bounded organelles (MBOs) are delivered to different domains in neurons by fast axonal transport. The importance of kinesin for fast anterograde transport is well established, but mechanisms for regulating kinesin-based motility are largely unknown. In this report, we provide biochemical and in vivo evidence that kinesin light chains (KLCs) interact with and are in vivo substrates for glycogen synthase kinase 3 (GSK3). Active GSK3 inhibited anterograde, but not retrograde, transport in squid axoplasm and reduced the amount of kinesin bound to MBOs. Kinesin microtubule binding and microtubule-stimulated ATPase activities were unaffected by GSK3 phosphorylation of KLCs. Active GSK3 was also localized preferentially to regions known to be sites of membrane delivery. These data suggest that GSK3 can regulate fast anterograde axonal transport and targeting of cargos to specific subcellular domains in neurons.
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