ANALYSIS OF CD36 BINDING DOMAINS - LIGAND SPECIFICITY CONTROLLED BY DEPHOSPHORYLATION OF AN ECTODOMAIN

被引：186

作者：

ASCH, AS ^{[1
]}

LIU, I ^{[1
]}

BRICCETTI, FM ^{[1
]}

BARNWELL, JW ^{[1
]}

KWAKYEBERKO, F ^{[1
]}

DOKUN, A ^{[1
]}

GOLDBERGER, J ^{[1
]}

PERNAMBUCO, M ^{[1
]}

机构：

[1] NYU,SCH MED,DEPT MOLEC PARASITOL,NEW YORK,NY 10010

来源：

SCIENCE | 1993年 / 262卷 / 5138期

关键词：

D O I：

10.1126/science.7504322

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：1436 / 1440

页数：5

共 31 条

[1]

ASCH A, UNPUB

[2] THROMBOSPONDIN SEQUENCE MOTIF (CSVTCG) IS RESPONSIBLE FOR CD36-BINDING [J].