ANCHORING MECHANISMS FOR LFA-3 CELL-ADHESION GLYCOPROTEIN AT MEMBRANE-SURFACE
ANCHORING MECHANISMS FOR LFA-3 CELL-ADHESION GLYCOPROTEIN AT MEMBRANE-SURFACE
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DOI：
10.1038/329846a0
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发表时间：
1987-10-29
期刊：
影响因子：
64.8
通讯作者：
SPRINGER, TA
中科院分区：
文献类型：
--
作者：
DUSTIN, ML;SELVARAJ, P;SPRINGER, TA
膜蛋白锚定在脂质双分子层上的方式可能对其功能有深远的影响。大多数细胞膜蛋白是由多肽链的跨膜片段锚定的，但也有几种蛋白质被描述为另一种类型的锚定：附着在蛋白质C末端的磷脂酰肌醇聚糖片段1,2。这种类型的连锁已经在参与粘附3和跨膜信号传导4,5的膜蛋白上被发现，并且在这些功能的执行中可能是重要的。我们在这里报道了一种重要的免疫粘附糖蛋白，淋巴细胞功能相关抗原3 (LFA-3)，可以通过两种类型的机制锚定在膜上。这两种不同的LFA-3细胞表面形式来源于不同的生物合成前体。磷脂酰肌醇连接和跨膜锚定形式的LFA-3的存在对LFA-3的粘附和跨膜信号传导具有重要意义。
The manner in which a membrane protein is anchored to the lipid bilayer may have a profound influence on its function. Most cell surface membrane proteins are anchored by a membrane-spanning segment(s) of the polypeptide chain, but another type of anchor has been described for several proteins: a phosphatidyl inositol glycan moiety, attached to the protein C terminus1,2. This type of linkage has been identified on membrane proteins involved in adhesion3and transmembrane signalling4,5and could be important in the execution of these functions. We report here that an immunologically important adhesion glycoprotein, lymphocyte function-associated antigen 3 (LFA-3), can be anchored to the membrane by both types of mechanism. These two distinct cell-surface forms of LFA-3 are derived from different biosynthetic precursors. The existence of a phosphatidyl-inositol-linked and a transmembrane anchored form of LFA-3 has important implications for adhesion and transmembrane signalling by LFA-3.