Linked Life Data

9842910

Source:http://linkedlifedata.com/resource/pubmed/id/9842910

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1998-12-17
pubmed:abstractText
A large fraction of glycosylphosphatidylinositol (GPI)-anchored proteins and Src-like kinases are confined to glycolipid-enriched membrane (GEM) microdomains. The particular membrane topology of GPI-anchored proteins has led to the postulation of the existence of integral membrane proteins linking extracellular stimuli with cytosolic machinery for endocytosis and signaling. The human MAL cDNA was identified during a search for novel genes differentially expressed during T cell development, and encodes a multispanning membrane protein displaying lipid-like properties. To address the biochemical characterization of endogenous MAL and to analyze its possible association with other proteins, we have generated a monoclonal antibody (mAb) specific to the MAL molecule. Using this mAb, we have identified MAL in GEM microdomains of both the HPB-ALL T cell line and human peripheral blood lymphocytes. Co-immunoprecipitation experiments with antibodies to the MAL molecule or to the GPI-anchored CD59 antigen indicated specific association of MAL with GPI-anchored proteins and Src-like tyrosine kinases. In addition, both MAL and the Src-like kinase Lck were identified in GEM obtained from an endosomal-enriched membrane fraction. These features of MAL closely match some of the properties expected for the hypothetical integral membrane linker proteins acting in specialized GEM-mediated functions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-2980
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3675-84
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
MAL, a novel integral membrane protein of human T lymphocytes, associates with glycosylphosphatidylinositol-anchored proteins and Src-like tyrosine kinases.
pubmed:affiliation
Centro de Biología Molecular Severo Ochoa, Universidad Autónoma de Madrid and Consejo Superior de Investigaciones Cientificas, Cantoblanco, Madrid, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't