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Titolo:
rlk/TXK encodes two forms of a novel cysteine string tyrosine kinase activated by Src family kinases
Autore:
Debnath, J; Chamorro, M; Czar, MJ; Schaeffer, EM; Lenardo, MJ; Varmus, HE; Schwartzberg, PL;
Indirizzi:
NCI, NIH, Bethesda, MD 20892 USA NCI Bethesda MD USA 20892NCI, NIH, Bethesda, MD 20892 USA Howard Hughes Med Inst, Res Scholars Program, NIH, Bethesda, MD 20892 USA Howard Hughes Med Inst Bethesda MD USA 20892 NIH, Bethesda, MD 20892 USA Natl Inst Human Genome Res, NIH, Bethesda, MD 20892 USA Natl Inst Human Genome Res Bethesda MD USA 20892 , Bethesda, MD 20892 USA NIAID, NIH, Bethesda, MD 20892 USA NIAID Bethesda MD USA 20892NIAID, NIH, Bethesda, MD 20892 USA George Washington Inst Biomed Sci, Washington, DC USA George Washington Inst Biomed Sci Washington DC USA , Washington, DC USA
Titolo Testata:
MOLECULAR AND CELLULAR BIOLOGY
fascicolo: 2, volume: 19, anno: 1999,
pagine: 1498 - 1507
SICI:
0270-7306(199902)19:2<1498:RETFOA>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
RI CROSS-LINKING; BRUTON TYROSINE; PROTEIN; PHOSPHORYLATION; PALMITOYLATION; ASSOCIATION; MEMBRANES; ITK; LCK; TRANSLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Schwartzberg, PL NIH, Natl Human Genome Res Inst, 49-4A38, Bethesda, MD 20892 USA NIH 49-4A38 Bethesda MD USA 20892 Bethesda, MD 20892 USA
Citazione:
J. Debnath et al., "rlk/TXK encodes two forms of a novel cysteine string tyrosine kinase activated by Src family kinases", MOL CELL B, 19(2), 1999, pp. 1498-1507

Abstract

Rlk/Txk is a member of the BTK/Tec family of tyrosine kinases and is primarily expressed in T lymphocytes. Unlike other members of this kinase family, Rlk lacks a pleckstrin homology (PH) domain near the amino terminus and instead contains a distinctive cysteine string motif We demonstrate here that Rlk protein consists of two isoforms that arise by alternative initiationof translation from the same cDNA. The shorter, internally initiated protein species lacks the cysteine string motif and is located in the nucleus when expressed in the absence of the larger form. In contrast, the larger form is cytoplasmic We show that the larger form is palmitoylated and that mutation of its cysteine string motif both abolishes palmitoylation and allowsthe protein to migrate to the nucleus, The cysteine string, therefore, is a critical determinant of both fatty acid modification and protein localization for the larger isoform of Rlk, suggesting that Rlk regulation is distinct from the other Btk family kinases, We further show that Rlk is phosphorylated and changes localization in response to T-cell-receptor (TCP) activation and, like the other Btk family kinases, can be phosphorylated and activated by Src family kinases, However, unlike the other Btk family members, Rlk is activated independently of the activity of phosphatidylinositol 3-kinase, consistent with its lack of a PA domain. Thus, Rlk has tao distinct isoforms, each of which may have unique properties in signaling downstream from the TCR.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 09:33:56