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G protein beta gamma subunit interaction with the dynein light-chain component Tctex-1 regulates neurite outgrowth.


ABSTRACT: Tctex-1, a light-chain component of the cytoplasmic dynein motor complex, can function independently of dynein to regulate multiple steps in neuronal development. However, how dynein-associated and dynein-free pools of Tctex-1 are maintained in the cell is not known. Tctex-1 was recently identified as a Gbetagamma-binding protein and shown to be identical to the receptor-independent activator of G protein signaling AGS2. We propose a novel role for the interaction of Gbetagamma with Tctex-1 in neurite outgrowth. Ectopic expression of either Tctex-1 or Gbetagamma promotes neurite outgrowth whereas interfering with their function inhibits neuritogenesis. Using embryonic mouse brain extracts, we demonstrate an endogenous Gbetagamma-Tctex-1 complex and show that Gbetagamma co-segregates with dynein-free fractions of Tctex-1. Furthermore, Gbeta competes with the dynein intermediate chain for binding to Tctex-1, regulating assembly of Tctex-1 into the dynein motor complex. We propose that Tctex-1 is a novel effector of Gbetagamma, and that Gbetagamma-Tctex-1 complex plays a key role in the dynein-independent function of Tctex-1 in regulating neurite outgrowth in primary hippocampal neurons, most likely by modulating actin and microtubule dynamics.

SUBMITTER: Sachdev P 

PROVIDER: S-EPMC1888676 | biostudies-literature | 2007 Jun

REPOSITORIES: biostudies-literature

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G protein beta gamma subunit interaction with the dynein light-chain component Tctex-1 regulates neurite outgrowth.

Sachdev Pallavi P   Menon Santosh S   Kastner David B DB   Chuang Jen-Zen JZ   Yeh Ting-Yu TY   Conde Cecilia C   Caceres Alfredo A   Sung Ching-Hwa CH   Sakmar Thomas P TP  

The EMBO journal 20070510 11


Tctex-1, a light-chain component of the cytoplasmic dynein motor complex, can function independently of dynein to regulate multiple steps in neuronal development. However, how dynein-associated and dynein-free pools of Tctex-1 are maintained in the cell is not known. Tctex-1 was recently identified as a Gbetagamma-binding protein and shown to be identical to the receptor-independent activator of G protein signaling AGS2. We propose a novel role for the interaction of Gbetagamma with Tctex-1 in n  ...[more]

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