Linked Life Data

11806999

Source:http://linkedlifedata.com/resource/pubmed/id/11806999

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2002-1-24
pubmed:abstractText
CD150 signaling lymphocytic activation molecule (SLAM), a T/B/dendritic cell surface glycoprotein, is a costimulatory receptor involved in T-cell activation and is also a receptor for measles virus. CD150-induced signal transduction is controlled by SAP/SH2D1A, the gene that is aberrant in X-linked lymphoproliferative disease and familial hemophagocytic lymphohistiocytosis. This report shows that CD150 colocalizes with the T-cell receptor (TCR) following CD3 triggering in human peripheral blood T cells and is rapidly and reversibly tyrosine phosphorylated on TCR cross-linking. The Src-like kinases Lck and Fyn phosphorylate tyrosine residues in the cytoplasmic tail of CD150. The results demonstrate that the SAP protein has 2 modes of binding to CD150. Binding to the motif Thr-Ile-Tyr281Ala-Gln-Val occurs in a phosphotyrosine-independent fashion and to the motif Thr-Val-Tyr327Ala-Ser-Val in a phosphotyrosine-dependent manner. Within both SAP binding motifs the threonine residue at position -2 to tyrosine is essential to stabilize the interaction irrespective of tyrosine phosphorylation, a feature unique to the SAP SH2 domain. A leucine residue, Leu278, further stabilizes nonphospho binding of SAP to Tyr281 of CD150. SAP blocking of the tyrosine phosphatase SHP-2 occurs primarily on Tyr281 of CD150 because SHP-2 requires both Tyr281 and Tyr327 for binding to CD150, and SAP binds to nonphosphorylated Tyr281. CD150 exhibits lateral mobility, segregating into intercellular contacts. The lateral mobility and homophilic clustering of CD150 between neighboring cells is not dependent on SAP/CD150 interaction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-4971
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
99
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
957-65
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11806999-Amino Acid Sequence, pubmed-meshheading:11806999-Animals, pubmed-meshheading:11806999-Antigens, CD, pubmed-meshheading:11806999-Binding Sites, pubmed-meshheading:11806999-COS Cells, pubmed-meshheading:11806999-Carrier Proteins, pubmed-meshheading:11806999-Glycoproteins, pubmed-meshheading:11806999-Humans, pubmed-meshheading:11806999-Immunoglobulins, pubmed-meshheading:11806999-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:11806999-Jurkat Cells, pubmed-meshheading:11806999-Molecular Sequence Data, pubmed-meshheading:11806999-Phosphorylation, pubmed-meshheading:11806999-Protein Binding, pubmed-meshheading:11806999-Protein-Tyrosine Kinases, pubmed-meshheading:11806999-Receptors, Antigen, T-Cell, pubmed-meshheading:11806999-Receptors, Cell Surface, pubmed-meshheading:11806999-Signal Transduction, pubmed-meshheading:11806999-T-Lymphocytes, pubmed-meshheading:11806999-Transfection, pubmed-meshheading:11806999-src Homology Domains
pubmed:year
2002
pubmed:articleTitle
Molecular dissection of the signaling and costimulatory functions of CD150 (SLAM): CD150/SAP binding and CD150-mediated costimulation.
pubmed:affiliation
Division of Immunology, RE-204, Beth Israel Deaconess Medical Center, Harvard Medical School, 330 Brookline Ave., Boston, MA 02215, USA. dhowie@caregroup.harvard.edu
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't