GSK‐3β Phosphorylation of Cytoplasmic Dynein Reduces Ndel1 Binding to Intermediate Chains and Alters Dynein Motility

Publisher: John Wiley & Sons Inc

E-ISSN: 1600-0854|16|9|941-961

ISSN: 1398-9219

Source: TRAFFIC (ELECTRONIC), Vol.16, Iss.9, 2015-09, pp. : 941-961

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Abstract

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.