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Titolo:
REGULATION OF CROSS-LINKING OF ACTIN FILAMENT BY IQGAP1, A TARGET FORCDC42
Autore:
FUKATA M; KURODA S; FUJII K; NAKAMURA T; SHOJI I; MATSUURA Y; OKAWA K; IWAMATSU A; KIKUCHI A; KAIBUCHI K;
Indirizzi:
NARA INST SCI & TECHNOL,DIV SIGNAL TRANSDUCT IKOMA 63001 JAPAN NARA INST SCI & TECHNOL,DIV SIGNAL TRANSDUCT IKOMA 63001 JAPAN HIROSHIMA UNIV,SCH DENT,DEPT BIOCHEM HIROSHIMA 734 JAPAN PRECURSORY RES EMBRYON SCI & TECHNOL,INHERITANCE & VARIAT GRP KYOTO 61902 JAPAN NATL INST INFECT DIS,DIV VIROL 2 TOKYO 162 JAPAN KIRIN BREWERY CO LTD,CENT LABS KEY TECHNOL YOKOHAMA KANAGAWA 236 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 47, volume: 272, anno: 1997,
pagine: 29579 - 29583
SICI:
0021-9258(1997)272:47<29579:ROCOAF>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
RASGAP-RELATED PROTEIN; RHO-FAMILY GTPASES; BINDING PROTEIN; PUTATIVE TARGET; ALPHA-ACTININ; F-ACTIN; KINASE; IDENTIFICATION; CALMODULIN; EFFECTOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
M. Fukata et al., "REGULATION OF CROSS-LINKING OF ACTIN FILAMENT BY IQGAP1, A TARGET FORCDC42", The Journal of biological chemistry, 272(47), 1997, pp. 29579-29583

Abstract

We have previously shown that IQGAP1, a recently identified target for Cdc42 and Rad small GTPases, showed a distribution similar to that of cortical actin cytoskeleton at the membrane ruffling area induced byinsulin and Rac1(val12) (Kuroda, S., Fukata, M,, Kobayashi, K., Nakafuku, M., Nomura, N., Iwamatsu, A., and Kaibuchi, K. (1996) J. Biol. Chem. 271, 28363-23367). Here we identified an IQGAP1-interacting molecule with molecular mass of 43 kDa (p43) from bovine brain cytosol, using glutathione S-transferase (GST)-IQGAP1 affinity column chromatography. The amino acid sequencing of the protein revealed that p43 was identical to beta- and gamma-actin. IQGAP1 was cosedimentated with filamentous actin (F-actin). The amino-terminal domain (amino acids 1-216) ofIQGAP1 was responsible for the interaction with F-actin. Falling ballviscometry assay revealed that IQGAP1 cross-linked the F-actin. This IQGAP1 activity was further enhanced by guanosine 5'-(3-O-thio)triphosphate (GTP gamma S) GST-Cdc42 but not by GDP-GST-Cdc42. The gel filtration analysis of IQGAP1 revealed that IQGAP1 appeared as oligomers andthat GTP gamma S-GST-Cdc42 but not GDP GST-Cdc42 enhanced the oligomerization of IQGAP1. These results strongly suggest that IQGAP1, actingdownstream of Cdc42, can cross-link the actin filament through its oligomerization.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 02:54:44