title: RGS2 promotes formation of neurites by stimulating microtubule polymerization.
abstract: Regulator of G-protein signaling (RGS) proteins interact with alpha 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.
authors.affiliation: Division of Molecular and Life Science, Pohang University of Science and Technology, Pohang, Kyungbuk 790-784, South Korea.
authors.forename: Kyun
authors.initials: K
authors.lastname: Heo
authors.forename: Sang Hoon
authors.initials: SH
authors.lastname: Ha
authors.forename: Young Chan
authors.initials: YC
authors.lastname: Chae
authors.forename: Sukmook
authors.initials: S
authors.lastname: Lee
authors.forename: Yong-Seok
authors.initials: YS
authors.lastname: Oh
authors.forename: Yun-Hee
authors.initials: YH
authors.lastname: Kim
authors.forename: Sun-Hee
authors.initials: SH
authors.lastname: Kim
authors.forename: Jung Hwan
authors.initials: JH
authors.lastname: Kim
authors.forename: Akira
authors.initials: A
authors.lastname: Mizoguchi
authors.forename: Tomohiko J
authors.initials: TJ
authors.lastname: Itoh
authors.forename: H Moo
authors.initials: HM
authors.lastname: Kwon
authors.forename: Sung Ho
authors.initials: SH
authors.lastname: Ryu
authors.forename: Pann-Ghill
authors.initials: PG
authors.lastname: Suh
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites / Q000235:genetics; D001921:Brain / Q000378:metabolism; D019556:COS Cells; D002454:Cell Differentiation / Q000235:genetics / Q000502:physiology; D002522:Chlorocebus aethiops; D005982:Glutathione Transferase / Q000235:genetics / Q000378:metabolism; D049452:Green Fluorescent Proteins / Q000235:genetics / Q000378:metabolism; D018613:Microscopy, Confocal; D008854:Microscopy, Electron; D008870:Microtubules / Q000378:metabolism* / Q000648:ultrastructure; D009154:Mutation / Q000235:genetics; D016501:Neurites / Q000378:metabolism / Q000502:physiology* / Q000648:ultrastructure; D016716:PC12 Cells; D011485:Protein Binding; D020710:RGS Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D034622:RNA Interference / Q000502:physiology; D034741:RNA, Small Interfering / Q000235:genetics; D051381:Rats; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014162:Transfection / Q000379:methods; D014404:Tubulin / Q000235:genetics / Q000378:metabolism; D014709:Vero Cells
chemical_list: D020710:RGS Proteins; D034741:RNA, Small Interfering; D011993:Recombinant Fusion Proteins; D014404:Tubulin; D049452:Green Fluorescent Proteins; D005982:Glutathione Transferase