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Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesin-based motilityMembrane-bounded organelles (MBOs) are delivered to different domains in neurons by fast axonal transport. The importance of kinesin for fast antero grade 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.
Document ID
20040088495
Document Type
Reprint (Version printed in journal)
External Source(s)
Authors
Morfini, Gerardo (University of Texas Southwestern Medical Center Dallas, TX 75390-9039, United States)
Szebenyi, Gyorgyi
Elluru, Ravindhra
Ratner, Nancy
Brady, Scott T.
Date Acquired
August 21, 2013
Publication Date
February 1, 2002
Publication Information
Publication: The EMBO journal
Volume: 21
Issue: 3
ISSN: 0261-4189
Subject Category
Life Sciences (General)
Funding Number(s)
CONTRACT_GRANT: NS23320
CONTRACT_GRANT: NS41170
CONTRACT_GRANT: NS23868
CONTRACT_GRANT: AG12646
Distribution Limits
Public
Copyright
Other
Keywords
NASA Discipline Neuroscience
Non-NASA Center