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Titolo:
COASSOCIATION OF RAP1A AND HA-RAS WITH RAF-1 N-TERMINAL REGION INTERFERES WITH RAS-DEPENDENT ACTIVATION OF RAF-1
Autore:
HU CD; KARIYA K; KOTANI G; SHIROUZU M; YOKOYAMA S; KATAOKA T;
Indirizzi:
KOBE UNIV,SCH MED,DEPT PHYSIOL 2,CHUO KU,7-5-1 KUSUNOKI CHO KOBE HYOGO 650 JAPAN KOBE UNIV,SCH MED,DEPT PHYSIOL 2,CHUO KU KOBE HYOGO 650 JAPAN RIKEN,INST PHYS & CHEM RES,CELLULAR SIGNALING LAB WAKO SAITAMA 35101 JAPAN UNIV TOKYO,SCH SCI,DEPT BIOCHEM & BIOPHYS,BUNKYO KU TOKYO 113 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 18, volume: 272, anno: 1997,
pagine: 11702 - 11705
SICI:
0021-9258(1997)272:18<11702:CORAHW>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-RESIDUES; SUPPRESSOR ACTIVITY; EFFECTOR REGION; IDENTIFICATION; PROTEINS; GENE; TRANSFORMATION; MUTATIONS; P21(RAS); C-RAF-1;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
27
Recensione:
Indirizzi per estratti:
Citazione:
C.D. Hu et al., "COASSOCIATION OF RAP1A AND HA-RAS WITH RAF-1 N-TERMINAL REGION INTERFERES WITH RAS-DEPENDENT ACTIVATION OF RAF-1", The Journal of biological chemistry, 272(18), 1997, pp. 11702-11705

Abstract

Raf-1 is a major downstream effector of mammalian Ras. Binding of theeffector domain of Ras to the Ras binding domain of Raf-1 is essential for Ras-dependent Raf-1 activation. However, Rap1A, which has an identical effector domain to that of Ras, cannot activate Raf-1 and even antagonizes several Ras functions in vivo. Recently, we identified thecysteine-rich region (CRR) of Raf-1 as another Ras-binding domain. Ha-Ras proteins carrying mutations N26G and V45E, which failed to bind to CRR, also failed to activate Raf-1, Since these mutations replace Ras residues with those of Rap1A, we examined if Rap1A lacks the abilityto bind to CRR, Contrary to the expectation, Rap1A exhibited a greatly enhanced binding to CRR compared with Ha-Ras. Enhanced CRR binding was also found with Ha-Ras carrying another Rap1A-type mutation E31K. Both Rap1A and Ha Ras(E31K) mutant failed to activate Raf-1 and interfered with Ha-Ras-dependent activation of Raf-1 in Sf9 cells. Enhanced binding of Rap1A to CRR led to co-association of Rap1A and Ha-Ras with Raf-1 N-terminal region through binding to CRR and Ras-binding domain,respectively. These results suggest that Rap1A interferes with Ras dependent Raf-1 activation by inhibiting binding of Ras to Raf-1 CRR.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 22:52:01