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GSK‐3β Phosphorylation of Cytoplasmic Dynein Reduces Ndel1 Binding to Intermediate Chains and Alters Dynein Motility
Author(s) -
Gao Feng J.,
Hebbar Sachin,
Gao Xu A.,
Alexander Michael,
Pandey Jai P.,
Walla Michael D.,
Cotham William E.,
King Stephen J.,
Smith Deanna S.
Publication year - 2015
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12304
Subject(s) - dynein , biology , microbiology and biotechnology , dynactin , gsk 3 , phosphorylation , dynein atpase , microtubule , motility , kinesin
A model for GSK ‐3β‐dependent regulation of retrograde organelle transport in response to insulin signaling. A) In control cells, active GSK ‐3 phosphorylates dynein. B) GSK ‐3 inactivation by insulin signaling or by inhibitors such as CT99021 ( CT ) or LiCl results in less phosphorylated dynein. Loss of phosphorylated residues in intermediate chains allows more efficient binding to Ndel1. Ndel1 stimulates dynein‐dependent cargo movement toward microtubule minus ends, suggesting a potential mechanism for regulation of retrograde organelle transport in response to extracellular cues.