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Titolo:
SPECIFIC DETECTION OF PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE BINDING-PROTEINS BY THE PIP3 ANALOG BEADS - AN APPLICATION FOR RAPID PURIFICATION OF THE PIP3 BINDING-PROTEINS
Autore:
SHIRAI T; TANAKA K; TERADA Y; SAWADA T; SHIRAI R; HASHIMOTO Y; NAGATA S; IWAMATSU A; OKAWA K; LI SW; HATTORI S; MANO H; FUKUI Y;
Indirizzi:
1-1-1 YAYOI CHO,BUNKYO KU TOKYO 1138657 JAPAN UNIV TOKYO,BIOCHEM LAB,DEPT APPL BIOL CHEM,GRAD SCH AGR & LIFE SCI TOKYO 1138657 JAPAN UNIV TOKYO,BIOORGAN CHEM LAB,INST MOL & CELLULAR BIOSCI TOKYO 1138657JAPAN KIRIN BREWERY CO LTD,CENT LABS KEY TECHNOL YOKOHAMA KANAGAWA 236 JAPAN JICHI MED SCH,DEPT BIOL MOL MINAMI KAWACHI TOCHIGI 32904 JAPAN NATL CTR NEUROL & PSYCHIAT,NATL INST NEUROSCI,DIV BIOCHEM & CELLULAR BIOL TOKYO 187 JAPAN
Titolo Testata:
Biochimica et biophysica acta. Molecular cell research
fascicolo: 3, volume: 1402, anno: 1998,
pagine: 292 - 302
SICI:
0167-4889(1998)1402:3<292:SDOP3B>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
TYROSINE KINASE; ACTIVATION; POLYPHOSPHOINOSITIDES; EXPRESSION; PATHWAY; DOMAIN; FAMILY;
Keywords:
PI3-KINASE; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE; PH DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
T. Shirai et al., "SPECIFIC DETECTION OF PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE BINDING-PROTEINS BY THE PIP3 ANALOG BEADS - AN APPLICATION FOR RAPID PURIFICATION OF THE PIP3 BINDING-PROTEINS", Biochimica et biophysica acta. Molecular cell research, 1402(3), 1998, pp. 292-302

Abstract

Phosphatidylinositol (PI) 3-kinase is known as one of the key molecules involved in the various biological events such as vesicle trafficking, cytoskeletal rearrangements and cell survival. To clarify the molecular basis underlying these events, we have tried to identify the proteins that can interact with phosphatidylinositol 3,3,5-trisphosphate (PIP3), the lipid product of PI3-kinase. Using a new PIP3 analogue, PIP3-APB, we synthesized an affinity column for PIP3 binding proteins. This enabled us to purify and identify several PIP3 binding proteins such as Tec tyrosine kinase, Gap1(m), and Akt, as the candidates for thedownstream molecules of PI3-kinase. All of these proteins contain PH domains, possible binding sites for phospholipids. Studies with various deletion mutants of Tec or Gap1(m) revealed that their PH domains are indeed the binding sites for PIP3. These results demonstrate that this PIP3 analogue binds various PIP3 binding proteins with high specificity and may be useful to elucidate the downstream mechanisms of PI3-kinases-mediated signaling pathways. (C) 1998 Elsevier Science B.V.

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Documento generato il 17/01/21 alle ore 18:10:37