What does S-palmitoylation do to membrane proteins?

被引:197
作者
Blaskovic, Sanja [1 ]
Blanc, Mathieu [1 ]
van der Goot, F. Gisou [1 ]
机构
[1] Ecole Polytech Fed Lausanne, Inst Global Hlth, CH-1015 Lausanne, Switzerland
基金
瑞士国家科学基金会;
关键词
DHHC; membrane proteins; palmitoylation; protein complexes; protein conformation; rafts; HUMAN BETA-2-ADRENERGIC RECEPTOR; CYSTEINE-RICH DOMAIN; CELL-SURFACE; DEPENDENT REGULATION; CYTOPLASMIC TAIL; RAS TRAFFICS; H-RAS; ASSOCIATION; EXPRESSION; PHOSPHORYLATION;
D O I
10.1111/febs.12263
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
S-palmitoylation is post-translational modification, which consists in the addition of a C16 acyl chain to cytosolic cysteines and which is unique amongst lipid modifications in that it is reversible. It can thus, like phosphorylation or ubiquitination, act as a switch. While palmitoylation of soluble proteins allows them to interact with membranes, the consequences of palmitoylation for transmembrane proteins are more enigmatic. We briefly review the current knowledge regarding the enzymes responsible for palmitate addition and removal. We then describe various observed consequences of membrane protein palmitoylation. We propose that the direct effects of palmitoylation on transmembrane proteins, however, might be limited to four non-mutually exclusive mechanistic consequences: alterations in the conformation of transmembrane domains, association with specific membrane domains, controlled interactions with other proteins and controlled interplay with other post-translational modifications.
引用
收藏
页码:2766 / 2774
页数:9
相关论文
共 85 条
[1]   Receptor palmitoylation and ubiquitination regulate anthrax toxin endocytosis [J].
Abrami, L ;
Leppla, SH ;
van der Goot, FG .
JOURNAL OF CELL BIOLOGY, 2006, 172 (02) :309-320
[2]   Palmitoylation and ubiquitination regulate exit of the Wnt signaling protein LRP6 from the endoplasmic reticulum [J].
Abrami, Laurence ;
Kunz, Beatrice ;
Lacovache, Ioan ;
Van der Goot, F. Gisou .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2008, 105 (14) :5384-5389
[3]  
[Anonymous], PLOS ONE
[4]   H-ras but not K-ras traffics to the plasma membrane through the exocytic pathway [J].
Apolloni, A ;
Prior, IA ;
Lindsay, M ;
Parton, RG ;
Hancock, JF .
MOLECULAR AND CELLULAR BIOLOGY, 2000, 20 (07) :2475-2487
[5]   Upregulated function of mitochondria-associated ER membranes in Alzheimer disease [J].
Area-Gomez, Estela ;
Castillo, Maria Del Carmen Lara ;
Tambini, Marc D. ;
Guardia-Laguarta, Cristina ;
de Groof, Ad J. C. ;
Madra, Moneek ;
Ikenouchi, Junichi ;
Umeda, Masato ;
Bird, Thomas D. ;
Sturley, Stephen L. ;
Schon, Eric A. .
EMBO JOURNAL, 2012, 31 (21) :4106-4123
[6]   Palmitoylation, pathogens and their host [J].
Blanc, Mathieu ;
Blaskovic, Sanja ;
van der Goot, F. Gisou .
BIOCHEMICAL SOCIETY TRANSACTIONS, 2013, 41 :84-88
[7]   Palmitoylation of CCR5 is critical for receptor trafficking and efficient activation of intracellular signaling pathways [J].
Blanpain, C ;
Wittamer, V ;
Vanderwinden, JM ;
Boom, A ;
Renneboog, B ;
Lee, B ;
Le Poul, E ;
El Asmar, L ;
Govaerts, C ;
Vassart, G ;
Doms, RW ;
Parmentier, M .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (26) :23795-23804
[8]   Palmitoylation of membrane proteins (Review) [J].
Charollais, Julie ;
Van Der Goot, F. Gisou .
MOLECULAR MEMBRANE BIOLOGY, 2009, 26 (1-2) :55-66
[9]   Live Cell Analysis of Aquaporin-4 M1/M23 Interactions and Regulated Orthogonal Array Assembly in Glial Cells [J].
Crane, Jonathan M. ;
Bennett, Jeffrey L. ;
Verkman, A. S. .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2009, 284 (51) :35850-35860
[10]   Mutation of juxtamembrane cysteines in the tetraspanin CD81 affects palmitoylation and alters interaction with other proteins at the cell surface [J].
Delandre, Caroline ;
Penabaz, Taryn R. ;
Passarelli, A. Lorena ;
Chapes, Stephen K. ;
Clem, Rollie J. .
EXPERIMENTAL CELL RESEARCH, 2009, 315 (11) :1953-1963