Lipids and topological rules governing membrane protein assembly.
Lipids and topological rules governing membrane protein assembly.
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DOI:
10.1016/j.bbamcr.2013.12.007
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发表时间:
2014-08
影响因子:
5.1
通讯作者:
Vitrac, Heidi
中科院分区:
文献类型:
--
作者:
Bogdanov, Mikhail;Dowhan, William;Vitrac, Heidi
关键词:
Membrane protein folding and topogenesis are tuned to a given lipid profile since lipids and proteins have co-evolved to follow a set of interdependent rules governing final protein topological organization. Transmembrane domain (TMD) topology is determined via a dynamic process in which topogenic signals in the nascent protein are recognized and interpreted initially by the translocon followed by a given lipid profile in accordance with the Positive Inside Rule. The net zero charged phospholipid phosphatidylethanolamine and other neutral lipids dampen the translocation potential of negatively charged residues in favor of the cytoplasmic retention potential of positively charged residues (Charge Balance Rule). This explains why positively charged residues are more potent topological signals than negatively charged residues. Dynamic changes in orientation of TMDs during or after membrane insertion are attributed to non-sequential cooperative and collective lipid–protein charge interactions as well as long-term interactions within a protein. The proportion of dual topological conformers of a membrane protein varies in a dose responsive manner with changes in the membrane lipid composition not only in vivo but also in vitro and therefore is determined by the membrane lipid composition. Switching between two opposite TMD topologies can occur in either direction in vivo and also in liposomes (designated as fliposomes) independent of any other cellular factors. Such lipid-dependent post-insertional reversibility of TMD orientation indicates a thermodynamically driven process that can occur at any time and in any cell membrane driven by changes in the lipid composition. This dynamic view of protein topological organization influenced by the lipid environment reveals previously unrecognized possibilities for cellular regulation and understanding of disease states resulting from mis-folded proteins. This article is part of a Special Issue entitled: Protein Trafficking & Secretion.
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DOI:
10.1016/j.bbalip.2012.08.007
发表时间:
2013-03
期刊:
Biochimica et biophysica acta
影响因子:
--
作者:
Dowhan W
通讯作者:
Dowhan W
影响因子:
4.8
作者:
BOGDANOV, M;DOWHAN, W
通讯作者:
DOWHAN, W
影响因子:
5.4
作者:
Dorobantu, Cristina;Macovei, Alina;Branza-Nichita, Norica
通讯作者:
Branza-Nichita, Norica
影响因子:
3.4
作者:
Dowhan, William;Bogdanov, Mikhail
通讯作者:
Bogdanov, Mikhail
DOI:
10.1016/b978-044453219-0.50003-9
发表时间:
2008-01-01
期刊:
BIOCHEMISTRY OF LIPIDS, LIPOPROTEINS AND MEMBRANES, 5TH EDITION
影响因子:
--
作者:
Dowhan, William;Bogdanov, Mikhail;Mileykovskaya, Eugenia
通讯作者:
Mileykovskaya, Eugenia