四斯潘宁
跨膜蛋白
棕榈酰化
细胞生物学
生物
跨膜结构域
膜蛋白
细胞质
生物化学
半胱氨酸
细胞
膜
受体
酶
作者
Christopher S. Stipp,Tatiana V. Kolesnikova,Martin E. Hemler
标识
DOI:10.1016/s0968-0004(02)00014-2
摘要
Abstract
Exciting new findings have emerged about the structure, function and biochemistry of tetraspanin proteins. Five distinct tetraspanin regions have now been delineated linking structural features to specific functions. Within the large extracellular loop of tetraspanins, there is a variable region that mediates specific interactions with other proteins, as well as a more highly conserved region that has been suggested to mediate homodimerization. Within the transmembrane region, the four tetraspanin transmembrane domains are probable sites of both intra- and inter-molecular interactions that are crucial during biosynthesis and assembly of the network of tetraspanin-linked membrane proteins known as the ‘tetraspanin web'. In the intracellular juxtamembrane region, palmitoylation of cysteine residues also contributes to tetraspanin web assembly, and the C-terminal cytoplasmic tail region could provide specific functional links to cytoskeletal or signaling proteins.
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