Submembraneous microtubule cytoskeleton: regulation of microtubule assembly by heterotrimeric G proteins
Heterotrimeric G proteins participate in signal transduction by transferring signals from cell surface receptors to intracellular effector molecules. G proteins also interact with microtubules and participate in microtubule-dependent centrosome/chromosome movement during cell division, as well as ne...
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Published in | The FEBS journal Vol. 275; no. 19; pp. 4654 - 4663 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Oxford, UK
Oxford, UK : Blackwell Publishing Ltd
01.10.2008
Blackwell Publishing Ltd |
Subjects | |
Online Access | Get full text |
ISSN | 1742-464X 1742-4658 |
DOI | 10.1111/j.1742-4658.2008.06614.x |
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Summary: | Heterotrimeric G proteins participate in signal transduction by transferring signals from cell surface receptors to intracellular effector molecules. G proteins also interact with microtubules and participate in microtubule-dependent centrosome/chromosome movement during cell division, as well as neuronal differentiation. In recent years, significant progress has been made in our understanding of the biochemical/functional interactions between G protein subunits (α and βγ) and microtubules, and the molecular details emerging from these studies suggest that α and βγ subunits of G proteins interact with tubulin/microtubules to regulate the assembly/dynamics of microtubules, providing a novel mechanism for hormone- or neurotransmitter-induced rapid remodeling of cytoskeleton, regulation of the mitotic spindle for centrosome/chromosome movements in cell division, and neuronal differentiation in which structural plasticity mediated by microtubules is important for appropriate synaptic connections and signal transmission. |
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Bibliography: | http://dx.doi.org/10.1111/j.1742-4658.2008.06614.x ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Literature Review-1 content type line 14 ObjectType-Article-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1742-464X 1742-4658 |
DOI: | 10.1111/j.1742-4658.2008.06614.x |