Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Distinct interactions of the X-linked lymphoproliferative syndrome gene product SAP with cytoplasmic domains of members of the CD2 receptor family
Autore:
Lewis, J; Eiben, LJ; Nelson, DL; Cohen, JI; Nichols, KE; Ochs, HD; Notarangelo, LD; Duckett, CS;
Indirizzi:
NCI, Metab Branch, Div Clin Sci, NIH, Bethesda, MD 20892 USA NCI BethesdaMD USA 20892 anch, Div Clin Sci, NIH, Bethesda, MD 20892 USA Univ Brescia, Dept Pediat, Ist Med Mol Angelo Nocivelli, Brescia, Italy Univ Brescia Brescia Italy Ist Med Mol Angelo Nocivelli, Brescia, Italy Univ Washington, Dept Pediat, Seattle, WA 98195 USA Univ Washington Seattle WA USA 98195 , Dept Pediat, Seattle, WA 98195 USA Childrens Hosp Philadelphia, Philadelphia, PA 19104 USA Childrens Hosp Philadelphia Philadelphia PA USA 19104 lphia, PA 19104 USA NIAID, Med Virol Sect, Clin Invest Lab, NIH, Bethesda, MD 20892 USA NIAIDBethesda MD USA 20892 Clin Invest Lab, NIH, Bethesda, MD 20892 USA
Titolo Testata:
CLINICAL IMMUNOLOGY
fascicolo: 1, volume: 100, anno: 2001,
pagine: 15 - 23
SICI:
1521-6616(200107)100:1<15:DIOTXL>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
EPSTEIN-BARR-VIRUS; TYROSINE-PHOSPHATASE; SIGNAL-TRANSDUCTION; IMMUNE-DEFICIENCY; IG SUPERFAMILY; ENCODING GENE; CUTTING EDGE; SH2 DOMAINS; PROTEIN SAP; KAPPA-B;
Keywords:
X-linked lymphoproliferative syndrome; Duncan's disease; SAP; SLAM; CD84;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Duckett, CS NCI, Metab Branch, Div Clin Sci, NIH, 10 Ctr Dr,Room 6B-05, Bethesda, MD 20892 USA NCI 10 Ctr Dr,Room 6B-05 Bethesda MD USA 20892 a, MD 20892 USA
Citazione:
J. Lewis et al., "Distinct interactions of the X-linked lymphoproliferative syndrome gene product SAP with cytoplasmic domains of members of the CD2 receptor family", CLIN IMMUNO, 100(1), 2001, pp. 15-23

Abstract

X-linked lymphoproliferative syndrome (XLP; Duncan's disease) is a primaryimmunodeficiency disease that manifests as an inability to regulate the immune response to Epstein-Barr virus (EBV) infection, Here we examine the ability of the product of the gene defective in XLP, SAP (DSHP/SH2D1A), to associate with the cytoplasmic domains of several members of the CD2 subfamily of cell surface receptors, including SLAM, 2B4, and CD84. While recruitment of SAP to SLAM occurred in a phosphorylation-independent manner, SAP wasfound to bind preferentially to tyrosine-phosphorylated cytoplasmic domains within 2B4 and CD84, Missense or nonsense mutations in the SAP open reading frame were identified in five of seven clinically diagnosed XLP patientsfrom different kindreds, Four of these variants retained the ability to bind to the cytoplasmic tails of SLAM and CD84, While ectopic expression of wild-type SAP was observed to block the binding of SHP-8 to SLAM, mutant SAPderivatives that retained the ability to bind SLAM did not inhibit recruitment of SHP-2 to SLAM, In contrast, SAP binding to CD84 had no effect on the ability of CD84 to recruit SHP-2, but instead displaced SHP-1 from the cytoplasmic tail of CD84, These results suggest that mutations in the gene encoding the XLP protein SAP lead to functional defects in the protein that include receptor binding and SHP-1 and SHP-8 displacement and that SAP utilizes different mechanisms to regulate signaling through the CD2 family of receptors, (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/07/20 alle ore 07:48:29