CD36 ectodomain phosphorylation blocks thrombospondin-1 binding: structure-function relationships and regulation by protein kinase C.


Abstract

New protein synthesis and trafficking through the Golgi are required for PMA-induced CD36 phosphorylation, suggesting that phosphorylation probably occurs intracellularly.

These studies suggest a novel in vivo pathway for CD36 phosphorylation that modulates cellular affinity for thrombospondin-related proteins to blunt vascular cell signaling.


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