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Titolo:
THE ACTIVITY OF D-RAF IN TORSO SIGNAL-TRANSDUCTION IS ALTERED BY SERINE SUBSTITUTION, N-TERMINAL DELETION, AND MEMBRANE TARGETING
Autore:
BAEK KH; FABIAN JR; SPRENGER F; MORRISON DK; AMBROSIO L;
Indirizzi:
IOWA STATE UNIV SCI & TECHNOL,DEPT ZOOL & GENET,SIGNAL TRANSDUCT TRAINING GRP AMES IA 50011 IOWA STATE UNIV SCI & TECHNOL,DEPT ZOOL & GENET,SIGNAL TRANSDUCT TRAINING GRP AMES IA 50011 NCI,MOL MECHANISMS CARCINOGENESIS LAB,ABL BASIC RES PROGRAM,FREDERICKCANC RES & DEV CTR FREDERICK MD 21702 UNIV CALIF SAN FRANCISCO,DEPT BIOCHEM & BIOPHYS SAN FRANCISCO CA 94143
Titolo Testata:
Developmental biology
fascicolo: 2, volume: 175, anno: 1996,
pagine: 191 - 204
SICI:
0012-1606(1996)175:2<191:TAODIT>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE; DROSOPHILA EMBRYO; TYROSINE KINASE; PHOSPHORYLATION; ONCOGENE; RECEPTOR; EXPRESSION; MELANOGASTER; REQUIREMENT; ACTIVATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
86
Recensione:
Indirizzi per estratti:
Citazione:
K.H. Baek et al., "THE ACTIVITY OF D-RAF IN TORSO SIGNAL-TRANSDUCTION IS ALTERED BY SERINE SUBSTITUTION, N-TERMINAL DELETION, AND MEMBRANE TARGETING", Developmental biology, 175(2), 1996, pp. 191-204

Abstract

The Raf family of serine/threonine kinases are essential components in many receptor tyrosine kinase-mediated signal transduction pathways. Here, we analyze the function of D-raf in the Torso (Tor) pathway required to specify cellular fates at the embryonic poles. Using mutant embryos lacking endogenous D-raf protein, we show that D-raf's serine/threonine kinase activity is essential for its role in Tor signal transduction and that human Raf-l will substitute for D-raf in this pathway. After Tor activation, D-raf becomes hyperphosphorylated. We identified two putative serine phosphorylation sites (S388 and S743) in SF9 cells and demonstrate that S743 or its phosphorylation is essential for D-raf function in embryos. Alanine substitution at S388, N-terminal truncation, or targeted membrane association permits transmission of theTorso signal by D-raf, but these D-raf molecules differ in their rescuing potential and relative biological activity. Membrane-targeted D-raf(tor4021) showed the highest level of activity, followed by alanine-substituted D-raf(S388A) and N-terminal-truncated D-raf(Delta 445). Since the activity profiles for these altered forms of D-raf are distinct, these findings indicate that each structural modification differentially affects the regulation and/or propagation of the Tor signal by these mutant D-raf proteins. (C) 1996 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 04:33:22