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Titolo:
SH2 SH3 ADAPTER PROTEINS CAN LINK TYROSINE KINASES TO A STE20-RELATEDPROTEIN-KINASE, HPK1/
Autore:
ANAFI M; KIEFER F; GISH GD; MBAMALU G; ISCOVE NN; PAWSON T;
Indirizzi:
MT SINAI HOSP,SAMUEL LUNENFELD RES INST,PROGRAMME MOL BIOL & CANC,600UNIV AVE TORONTO ON M5G 1X5 CANADA MT SINAI HOSP,SAMUEL LUNENFELD RES INST,PROGRAMME MOL BIOL & CANC TORONTO ON M5G 1X5 CANADA UNIV TORONTO,DEPT MOL & MED GENET TORONTO ON M5S 1A8 CANADA UNIV TORONTO,ONTARIO CANC INST TORONTO ON M5G 2M9 CANADA UNIV TORONTO,DEPT MED BIOPHYS TORONTO ON M5G 2M9 CANADA
Titolo Testata:
The Journal of biological chemistry
fascicolo: 44, volume: 272, anno: 1997,
pagine: 27804 - 27811
SICI:
0021-9258(1997)272:44<27804:SSAPCL>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
SH3 DOMAIN; CELL-DEATH; SH3-LIGAND INTERACTIONS; GENERAL-MODEL; CRK ADAPTER; BINDING; STRESS; PATHWAY; ACTIVATION; APOPTOSIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
57
Recensione:
Indirizzi per estratti:
Citazione:
M. Anafi et al., "SH2 SH3 ADAPTER PROTEINS CAN LINK TYROSINE KINASES TO A STE20-RELATEDPROTEIN-KINASE, HPK1/", The Journal of biological chemistry, 272(44), 1997, pp. 27804-27811

Abstract

Ste20-related protein kinases have been implicated as regulating a range of cellular responses, including stress-activated protein kinase pathways and the control of cytoskeletal architecture. An important issue involves the identities of the upstream signals and regulators thatmight control the biological functions of mammalian Ste20-related protein kinases. HPK1 is a protein-serine/threonine kinase that possessesa Ste20-like kinase domain, and in transfected cells activates a protein kinase pathway leading to the stress-activated protein kinase SAPK/JNK. Here we have investigated candidate upstream regulators that might interact with HPK1. HPK1 possesses an N-terminal catalytic domain and an extended C-terminal tail with four proline-rich motifs. The SH3 domains of Grb2 bound in vitro to specific proline-rich motifs in the HPK1 tail and functioned synergistically to direct the stable binding of Grb2 to HPK1 in transfected Cos1 cells. Epidermal growth factor (EGF) stimulation did not affect the binding of Grb2 to HPK1 but induced recruitment of the Grb2-HPK1 complex to the autophosphorylated EGF receptor and to the Shc docking protein. Several activated receptor and cytoplasmic tyrosine kinases, including the EGF receptor, stimulated the tyrosine phosphorylation of the HPK1 serine/threonine kinase. These results suggest that HPK1, a mammalian Ste20-related protein-serine/threonine kinase, can potentially associate with protein-tyrosine kinases through interactions mediated by SH2/SH3 adaptors such as Grb2. Suchinteraction may provide a possible mechanism for cross-talk between distinct biochemical pathways following the activation of tyrosine kinases.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 06:50:04