Journal Article10.1038/NRM2084
Palmitoylation: policing protein stability and traffic
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TL;DR: Recent studies that have provided insights into the mechanisms that mediate the functional consequences of palmitate are reviewed.
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Abstract: Palmitate modifies both peripheral and integral membrane proteins and its addition can be permanent or transient, which makes it unique among the lipid modifications of proteins. The presence of palmitate on a protein affects how the protein interacts with lipids and proteins in a membrane compartment, and the reversibility of palmitoylation allows different modes of trafficking between membrane compartments. Here, we review recent studies that have provided insights into the mechanisms that mediate the functional consequences of this versatile modification.
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Citations
Purification and reconstitution of sterol transfer by native mouse ABCG5 and ABCG8.
TL;DR: The purification of endogenous G5G8 from mouse liver to near homogeneity was described and it was reported that G5 but not G8 is S-palmitoylated and that palmitoylation is not essential for dimerization, trafficking, or biliary sterol secretion.
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Palmitoylation controls trafficking of the intracellular Ca2+ channel MCOLN3/TRPML3 to regulate autophagy.
So Woon Kim,Donghyun Kim,Kyoung Sun Park,Mi Kyung Kim,Yun Min Park,Shmuel Muallem,Insuk So,Hyunjin Kim +7 more
TL;DR: The results suggest that trafficking and channel function of MCOLN3/TRPML3 are regulated in the context of autophagy, and palmitoylation is a prerequisite for the function of the channel as a Ca2+ channel in autophagosome formation by controlling its trafficking between subcellular compartments.
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Synaptic plasticity regulated by protein-protein interactions and posttranslational modifications
TL;DR: This chapter reviews the current knowledge about the regulatory mechanisms for AMPAR trafficking and channel gating by protein-protein interactions and posttranslational modifications, and focuses on the recently established mode of action of the AMPAR auxiliary subunit, stargazin/TARPs, and PSD-95 scaffold.
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Lipid-Induced Conformational Switch Controls Fusion Activity of Longin Domain SNARE Ykt6
Wenyu Wen,Jiang Yu,Lifeng Pan,Zhiyi Wei,Jingwei Weng,Wenning Wang,Yan Shan Ong,Ton Hoai Thi Tran,Wanjin Hong,Mingjie Zhang,Mingjie Zhang +10 more
TL;DR: It is demonstrated that unlipidated Ykt6 adopts multiple conformations, with a small population in the closed state, and that the posttranslationally attached farnesyl group can actively regulate Ykt 6 fusion activity in addition to its anticipated membrane-anchoring role.
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Role of S-palmitoylation on IFITM5 for the interaction with FKBP11 in osteoblast cells.
Takashi Tsukamoto,Xianglan Li,Hiromi Morita,Takashi Minowa,Tomoyasu Aizawa,Nobutaka Hanagata,Nobutaka Hanagata,Makoto Demura +7 more
TL;DR: Investigating the role played by S-palmitoylation of IFITM5 in its interaction with FKBP11 in the cells and investigating bone nodule formation in osteoblast cells in the presence of 2BP indicated that the S-Palmitoylated contributes to bone formation.
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