http://www.cnr.it/ontology/cnr/individuo/prodotto/ID37851

Transmembrane topogenesis of a tail-anchored protein is modulated by membrane lipid composition. (Articolo in rivista)

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Transmembrane topogenesis of a tail-anchored protein is modulated by membrane lipid composition. (Articolo in rivista) (literal)

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Brambillasca S; Yabal M; Soffientini P; Stefanovic S; Makarow M; Hegde RS; Borgese N (2005)
Transmembrane topogenesis of a tail-anchored protein is modulated by membrane lipid composition.
in EMBO journal (Print); NATURE PUBLISHING GROUP,, LONDON (Regno Unito)
(literal)

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Brambillasca S; Yabal M; Soffientini P; Stefanovic S; Makarow M; Hegde RS; Borgese N (literal)

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Brambillasca S: Istituto di Neuroscienze del CNR e Dipartimento di Farmacologia Medica, Università di Milano; Yabal M: Program of Cellular Biotechnology, Institute of Biotechnology, and Department of Applied Chemistry and Microbiology, 00014 University of Helsinki, Helsinki, Finland; Soffientini P: Istituto di Neuroscienze del CNR e Dipartimento di Farmacologia Medica, Università di Mlano; Stefanovic S:Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA; Makarow M: Program of Cellular Biotechnology, Institute of Biotechnology, and 4Department of Applied Chemistry and Microbiology, 00014 University of Helsinki, Helsinki, Finland; Hegde RS: Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA; Borgese N: Istituto di Neuroscienze del CNR e Dipartimento di Farmacologia Medica, Università di Milano; Dipartimento di Scienze Farmacobiologiche, Università \"Magna Graecia\" di Catanzaro (literal)

Titolo

Transmembrane topogenesis of a tail-anchored protein is modulated by membrane lipid composition. (literal)

Abstract

A large class of proteins with cytosolic functional domains is anchored to selected intracellular membranes by a single hydrophobic segment close to the C-terminus. Although such tail-anchored (TA) proteins are numerous, diverse, and functionally important, the mechanism of their transmembrane insertion and the basis of their membrane selectivity remain unclear. To address this problem, we have developed a highly specific, sensitive, and quantitative in vitro assay for the proper membrane-spanning topology of a model TA protein, cytochrome b5 (b5). Selective depletion from membranes of components involved in cotranslational protein translocation had no effect on either the efficiency or topology of b5 insertion. Indeed, the kinetics of transmembrane insertion into protein-free phospholipid vesicles was the same as for native ER microsomes. Remarkably, loading of either liposomes or microsomes with cholesterol to levels found in other membranes of the secretory pathway sharply and reversibly inhibited b5 transmembrane insertion. These results identify the minimal requirements for transmembrane topogenesis of a TA protein and suggest that selectivity among various intracellular compartments can be imparted by differences in their lipid composition. (literal)

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