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Titolo:
HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 NEF BINDS DIRECTLY TO LCK AND MITOGEN-ACTIVATED PROTEIN-KINASE, INHIBITING KINASE-ACTIVITY
Autore:
GREENWAY A; AZAD A; MILLS J; MCPHEE D;
Indirizzi:
MACFARLANE BURNET CTR MED RES,NATL CTR HIV VIROL RES,AIDS CELLULAR BIOL UNIT,POB 254 FAIRFIELD VIC 3078 AUSTRALIA BIOMOL RES INST PARKVILLE VIC 3052 AUSTRALIA
Titolo Testata:
Journal of virology
fascicolo: 10, volume: 70, anno: 1996,
pagine: 6701 - 6708
SICI:
0022-538X(1996)70:10<6701:HTNBDT>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
BLOOD MONONUCLEAR-CELLS; AMINO-TERMINAL DOMAIN; HUMAN T-CELLS; NF-KAPPA-B; SIGNAL-TRANSDUCTION; SH3 DOMAINS; CYTOPLASMIC DOMAINS; TYROSINE KINASES; DOWN-REGULATION; MESSENGER-RNA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
57
Recensione:
Indirizzi per estratti:
Citazione:
A. Greenway et al., "HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 NEF BINDS DIRECTLY TO LCK AND MITOGEN-ACTIVATED PROTEIN-KINASE, INHIBITING KINASE-ACTIVITY", Journal of virology, 70(10), 1996, pp. 6701-6708

Abstract

It is now well established that human immunodeficiency virus type 1 (HIV-1) Nef contributes substantially to disease pathogenesis by augmenting virus replication and markedly perturbing T-cell function, The effect of Nef on host cell activation could be explained in part by its interaction with specific cellular proteins involved in signal transduction, including at least a member of the src family kinase, Lck, and the serine/threonine kinase, mitogen-activated protein kinase (MAPK). Recombinant Nef directly interacted with purified Lck and MAPK in coprecipitation experiments and binding assays, A proline rich repeat sequence [(Pxx)(4)] in Nef occurring between amino acid residues 69 to 78 is highly conserved and bears strong resemblance to a defined consensus sequence identified as an SH3 binding domain present in several proteins which can interact with the SH3 domain of various signalling and cytoskeletal proteins, Binding and coprecipitation assays with short synthetic peptides corresponding to the proline-rich repeat sequence [(Pxx)(4)] of Nef and the SH2, SH3, or SH2 and SH3 domains of Lck revealed that the interaction between these two proteins is at least in partmediated by the proline repeat sequence of Nef and the SH3 domain of Lck, In addition to direct binding to full-length Nef, MAPK was also shown to bind the same proline repeat motif, Nef protein significantly decreased the in vitro kinase activity of Lck and MAPK, Inhibition of key members of signalling cascades, including those emanating from theT-cell receptor, by the HIV-1 Nef protein undoubtedly alters the ability of the infected T cell to respond to antigens or cytokines, facilitating HIV-1 replication and contributing to HIV-l-induced disease pathogenesis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 09:03:35