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Titolo:
Membrane recruitment of DOCK180 by binding to Ptdlns(3,4,5)P-3
Autore:
Kobayashi, S; Shirai, T; Kiyokawa, E; Mochizuki, N; Matsuda, M; Fukui, Y;
Indirizzi:
Int Med Ctr Japan, Inst Res, Dept Pathol, Shinjuku Ku, Tokyo 1628655, Japan Int Med Ctr Japan Tokyo Japan 1628655 Shinjuku Ku, Tokyo 1628655, Japan Univ Tokyo, Grad Sch Agr & Life Sci, Dept Appl Biol Chem, Bunkyo Ku, Tokyo1130032, Japan Univ Tokyo Tokyo Japan 1130032 Biol Chem, Bunkyo Ku, Tokyo1130032, Japan Natl Inst Infect Dis, Dept Pathol, Shinjuku Ku, Tokyo 1628640, Japan Natl Inst Infect Dis Tokyo Japan 1628640 injuku Ku, Tokyo 1628640, Japan
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 354, anno: 2001,
parte:, 1
pagine: 73 - 78
SICI:
0264-6021(20010215)354:<73:MRODBB>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLECKSTRIN HOMOLOGY DOMAINS; RAT PC12 CELLS; PHOSPHATIDYLINOSITOL-3 KINASE; GUANOSINE TRIPHOSPHATASES; SIGNAL-TRANSDUCTION; PLASMA-MEMBRANE; MYOBLAST CITY; PH DOMAINS; PROTEIN; DBL;
Keywords:
CDM family proteins; pleckstrin homology domain; Rac;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Matsuda, M Int Med Ctr Japan, Inst Res, Dept Pathol, Shinjuku Ku, 1-21-1 Toyama, Tokyo 1628655, Japan Int Med Ctr Japan 1-21-1 Toyama Tokyo Japan 1628655 655, Japan
Citazione:
S. Kobayashi et al., "Membrane recruitment of DOCK180 by binding to Ptdlns(3,4,5)P-3", BIOCHEM J, 354, 2001, pp. 73-78

Abstract

DOCK180 was originally identified as one of two major proteins bound to the Crk oncogene product and became an archetype of the CDM family of proteins. including Ced-5 of Caenorhabditis elegans and Mbc of Drosophila melanogaster. Further study has suggested that DOCK180 is involved in the activation of Rac by the CrkII-p130(Cas) complex. With the use of deletion mutants of DOCK180. we found that the C-terminal region containing a cluster of basic amino acids was required for binding to and activation of Rac. This region showed high amino-acid sequence similarity to the consensus sequence of the phosphoinositide-binding site; this led us to examine whether this basicregion binds to phosphoinositides. For this purpose we used PtdIns(3,4,5)P-3-APB beads, as reported previously [Shirai, Tanaka, Terada, Sawada, Shirai, Hashimoto, Nagata, Iwamatsu, Okawa, Li et al. (1998) Biochim. Biophys. Acta 1402, 292-302]. By using various competitors, we demonstrated the specific binding of DOCK180 to PtdIns(3,3,5)P-3. The expression of active phosphoinositide 3-kinase (PI-3K) did not enhance a DOCK180-induced increase in GTP-Rac; however, the expression of PI-3K translocated DOCK180 to the plasmamembrane. Thus DOCK180 contained a phosphoinositide-binding domain, as didthe other guanine nucleotide exchange factors with a Db1 homology domain, and was translocated to the plasma membrane on the activation of PI-3K.

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Documento generato il 30/09/20 alle ore 09:31:33