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Titolo:
TYROSINE-112 OF LATENT MEMBRANE-PROTEIN 2A IS ESSENTIAL FOR PROTEIN-TYROSINE KINASE LOADING AND REGULATION OF EPSTEIN-BARR-VIRUS LATENCY
Autore:
FRUEHLING S; SWART R; DOLWICK KM; KREMMER E; LONGNECKER R;
Indirizzi:
NORTHWESTERN UNIV,SCH MED,DEPT MICROBIOL IMMUNOL,303 E CHICAGO AVE CHICAGO IL 60611 NORTHWESTERN UNIV,SCH MED,DEPT MICROBIOL IMMUNOL CHICAGO IL 60611 GSF MUNICH,INST IMMUNOL D-81377 MUNICH GERMANY
Titolo Testata:
Journal of virology
fascicolo: 10, volume: 72, anno: 1998,
pagine: 7796 - 7806
SICI:
0022-538X(1998)72:10<7796:TOLM2I>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-ANTIGEN RECEPTOR; PHOSPHORYLATED IG-ALPHA; LYN-DEFICIENT MICE; SIGNAL-TRANSDUCTION; SRC FAMILY; MARMOSET LEUKOCYTES; AUTOIMMUNE-DISEASE; ACTIVATION MOTIF; B-LYMPHOCYTES; TRANSFORMATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
48
Recensione:
Indirizzi per estratti:
Citazione:
S. Fruehling et al., "TYROSINE-112 OF LATENT MEMBRANE-PROTEIN 2A IS ESSENTIAL FOR PROTEIN-TYROSINE KINASE LOADING AND REGULATION OF EPSTEIN-BARR-VIRUS LATENCY", Journal of virology, 72(10), 1998, pp. 7796-7806

Abstract

Latent membrane protein 2A (LMP2A) of Epstein-Barr virus (EBV) is expressed on the plasma membrane of B lymphocytes latently infected with EBV and blocks B-cell receptor (BCR) signal transduction in EBV-immortalized B cells in vitro. The LMP2A amino-terminal domain that is essential for the LMP2A-mediated block on BCR signal transduction contains eight tyrosine residues. Association of Syk protein tyrosine kinase (PTK) with LMP2A occurs at the two tyrosines of the LMP2A immunoreceptortyrosine-based activation motif, and it is hypothesized that Lyn PTK associates with the YEEA amino acid motif at LMP2A tyrosine 112 (Y112). To examine the specific association of Lyn PTK to LMP2A, a panel of LMP2A cDNA expression vectors containing LMP2A mutations were transfected into an EBV-negative B-cell line and analyzed for Lyn and LMP2A coimmunoprecipitation. Lyn associates with wild-type LMP2A and other LMP2A mutant constructs, but Lyn association is lost in the LMP2A construct containing a tyrosine (Y)-to-phenylalanine (F) mutation at LMP2A residue Y112 (LMP2AY112F). Next, the LMP2AY112F mutation was recombined into the EBV genome to generate stable lymphoblastoid cell lines (LCLs) transformed with the LMP2AY112F mutant virus. Analysis of BCR-mediated signal transduction in the LMP2AY112F LCLs revealed loss of the LMP2A-mediated block in BCR signal transduction. In addition, LMP2A was not tyrosine phosphorylated in LMP2AY112F LCLs. Together these data indicate the importance of the LMP2A Y112 residue in the ability of LMP2Ato block BCR-mediated signal transduction and place the role of this residue and its interaction with Lyn PTK as essential to LMP2A phosphorylation, PTK loading, and down-modulation of PTKs involved in BCR-mediated signal transduction.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/08/20 alle ore 22:31:24