Palmitoylation regulates raft affinity for the majority of integral raft proteins
Palmitoylation regulates raft affinity for the majority of integral raft proteins
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DOI：
10.1073/pnas.1016184107
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发表时间：
2010-12-21
影响因子：
11.1
通讯作者：
Simons, Kai
中科院分区：
文献类型：
--
作者：
Levental, Ilya;Lingwood, Daniel;Simons, Kai
The physical basis for protein partitioning into lipid rafts remains an outstanding question in membrane biology that has previously been addressed only through indirect techniques involving differential solubilization by nonionic detergents. We have used giant plasma membrane vesicles, a plasma membrane model system that phase separates to include an ordered phase enriching for raft constituents, to measure the partitioning of the transmembrane linker for activation of T cells (LAT). LAT enrichment in the raft phase was dependent on palmitoylation at two juxtamembrane cysteines and could be enhanced by oligomerization. This palmitoylation requirement was also shown to regulate raft phase association for the majority of integral raft proteins. Because cysteine palmitoylation is the only lipid modification that has been shown to be reversibly regulated, our data suggest a role for palmitoylation as a dynamic raft targeting mechanism for transmembrane proteins.
