Journal article
Analysis of CD36 Binding Domains: Ligand Specificity Controlled by Dephosphorylation of an Ectodomain
Science (American Association for the Advancement of Science), Vol.262(5138), pp.1436-1440
11/26/1993
DOI: 10.1126/science.7504322
PMID: 7504322
Abstract
The protein CD36 is a membrane receptor for thrombospondin (TSP), malaria-infected erythrocytes, and collagen. Three functional sequences were identified within a single disulfide loop of CD36: one that mediates TSP binding (amino acids 87 to 99) and two that support malarial cytoadhesion (amino acids 8 to 21 and 97 to 110). One of these peptides (p87-99) is a consensus protein kinase C (PKC) phosphorylation site. Dephosphorylation. of constitutively phosphorylated CD36 in resting platelets and a megakaryocytic cell line led to the loss of collagen adhesion and platelet reactivity to collagen, with a reciprocal increase in TSP binding. PKC-mediated phosphorylation of this ectodomain resulted in a loss of TSP binding and the reciprocal acquisition of collagen binding. In site-directed mutagenesis studies, when the threonine phosphorylation site was changed to alanine, CD36 was expressed in a dephosphorylated state and bound to TSP constitutively.
Details
- Title: Subtitle
- Analysis of CD36 Binding Domains: Ligand Specificity Controlled by Dephosphorylation of an Ectodomain
- Creators
- Adam S. Asch - Cornell UniversityIsaac Liu - Cornell UniversityFrederick M. Briccetti - Cornell UniversityJohn W. Barnwell - New York UniversityFrank Kwakye-Berko - New York UniversityAyotunde Dokun - Cornell UniversityJeffrey Goldberger - Cornell UniversityMona Pernambuco - Cornell University
- Resource Type
- Journal article
- Publication Details
- Science (American Association for the Advancement of Science), Vol.262(5138), pp.1436-1440
- DOI
- 10.1126/science.7504322
- PMID
- 7504322
- ISSN
- 0036-8075
- eISSN
- 1095-9203
- Language
- English
- Date published
- 11/26/1993
- Academic Unit
- Molecular Physiology and Biophysics; Fraternal Order of Eagles Diabetes Research Center; Endocrinology and Metabolism; Internal Medicine
- Record Identifier
- 9984297596102771
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