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Titolo:
INTERACTIONS OF THE AMINO-ACID RESIDUE AT POSITION-31 OF THE C-HA-RASPROTEIN WITH RAF-1 AND RALGDS
Autore:
SHIROUZU M; MORINAKA K; KOYAMA S; HU CD; HORITAMURA N; OKADA T; KARIYA K; KATAOKA T; KIKUCHI A; YOKOYAMA S;
Indirizzi:
RIKEN,INST PHYS & CHEM RES,CELLULAR SIGNALING LAB,HIROSAWA 2-1 WAKO SAITAMA 35101 JAPAN RIKEN,INST PHYS & CHEM RES,CELLULAR SIGNALING LAB WAKO SAITAMA 35101 JAPAN HIROSHIMA UNIV,SCH MED,DEPT BIOCHEM 1,MINAMI KU HIROSHIMA 734 JAPAN KOBE UNIV,SCH MED,DEPT PHYSIOL 2,CHUO KU KOBE HYOGO 650 JAPAN UNIV TOKYO,GRAD SCH SCI,DEPT BIOCHEM & BIOPHYS,BUNKYO KU TOKYO 113 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 13, volume: 273, anno: 1998,
pagine: 7737 - 7742
SICI:
0021-9258(1998)273:13<7737:IOTARA>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEOTIDE DISSOCIATION STIMULATOR; SIGNAL-TRANSDUCTION; EFFECTOR REGION; R-RAS; IDENTIFICATION; BINDING; KINASE; GENE; TRANSFORMATION; DOWNSTREAM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
42
Recensione:
Indirizzi per estratti:
Citazione:
M. Shirouzu et al., "INTERACTIONS OF THE AMINO-ACID RESIDUE AT POSITION-31 OF THE C-HA-RASPROTEIN WITH RAF-1 AND RALGDS", The Journal of biological chemistry, 273(13), 1998, pp. 7737-7742

Abstract

The Ras and Rap1A proteins can bind to the Raf and RalGDS families. Ras and Rap1A have Glu and Lys, respectively, at position 31. In the present study, we analyzed the effects of mutating the Glu at position 31 of the c-Ha-Ras protein to Asp, Ala, Arg, and Lys on the interactions with Raf-1 and RalGDS. The Ras-binding domain (RBD) of Raf-1 binds the E31R and E31K Ras mutants less tightly than the wild-type, E31A, and E81D Ras proteins; the introduction of the positively charged Lys orArg residue at position 31 specifically impairs the binding of Ras with the Raf-1 RBD. On the other hand, the ability of the oncogenic Ras(G12V) protein to activate Raf-1 in HEK293 cells was only partially reduced by the E31R mutation but was drastically impaired by the E31K mutation. Correspondingly, Ras(G12V)(E31K) as well as Rap1A, but not Ras(G12V)(E31R), exhibited abnormally tight binding with the cysteine-richdomain of Raf-1. On the other hand, the E31A, E31R, and E31K mutations, but not the E31D mutation, enhanced the RalGDS RBD-binding activityof Ras, indicating that the negative charge at position 31 of Ras is particularly unfavorable to the interaction with the RalGDS RBD. Ras(G12V)(E31K), Ras(G12V)(E31A), and Rap1A stimulate the RalGDS action more efficiently than the wild-type Ras in the liposome reconstitution assay. All of these results clearly show that the sharp contrast betweenthe characteristics of Ras and Rap1A, with respect to the interactions with Raf-1 and RalGDS, depends on their residues at position 31.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/08/20 alle ore 16:25:27