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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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RGS2 promotes formation of neurites by stimulating microtubule polymerization

Cited 29 times inthomson ciCited 23 times inthomson ci
Title
RGS2 promotes formation of neurites by stimulating microtubule polymerization
Author
Heo, KyunHa, Sang HoonChae, Young ChanLee, SukmookOh, Yong-SeokKim, Yun-HeeKim, Sun-HeeKim, Jung HwanMizoguchi, AkiraItoh, Tomohiko J.Kwon, H. MooRyu, Sung HoSuh, Pann-Ghill
Issue Date
2006-12
Publisher
ELSEVIER SCIENCE INC
Citation
CELLULAR SIGNALLING, v.18, no.12, pp.2182 - 2192
Abstract
Regulator of G-protein signaling (RGS) proteins interact with α subunits of heterotrimeric G-proteins via the RGS domain and attenuate their activity by accelerating GTPase activity. RGS2, a member of the RGS family, regulates synaptic development via hereto unknown mechanism. In this study, we found that RGS2 directly interacted with tubulin via a short region at the N-terminus: amino acids 41-60. RGS2 enhanced microtubule polymerization in vitro, and the tubulin binding region was necessary and sufficient for this activity. In Vero cells, polymerization of microtubule was stimulated when peptides containing the tubulin binding region were microinjected. Immunocytochemical analysis showed that endogenous RGS2 was localized at the termini of neurites in differentiated PC12 cells. Over-expression of RGS2 enhanced the nerve growth factor-induced neurite outgrowth in PC12 cells, while specific knock-down of endogenous RGS2 suppressed the neurite outgrowth. These findings demonstrate that RGS2 contributes to the neuronal cell differentiation via regulation of microtubule dynamics.
URI
https://scholarworks.unist.ac.kr/handle/201301/4891
URL
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33750312906
DOI
10.1016/j.cellsig.2006.05.006
ISSN
0898-6568
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BIO_Journal Papers
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