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Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins

Standard

Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins. / Favaloro, Vincenzo; Spasic, Milan; Schwappach, Blanche; Dobberstein, Bernhard.

in: J CELL SCI, Jahrgang 121, Nr. 11, 01.06.2008, S. 1832-40.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Favaloro, V, Spasic, M, Schwappach, B & Dobberstein, B 2008, 'Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins', J CELL SCI, Jg. 121, Nr. 11, S. 1832-40. https://doi.org/10.1242/jcs.020321

APA

Favaloro, V., Spasic, M., Schwappach, B., & Dobberstein, B. (2008). Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins. J CELL SCI, 121(11), 1832-40. https://doi.org/10.1242/jcs.020321

Vancouver

Favaloro V, Spasic M, Schwappach B, Dobberstein B. Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins. J CELL SCI. 2008 Jun 1;121(11):1832-40. https://doi.org/10.1242/jcs.020321

Bibtex

@article{167f9e780bad4733ac28172528e53351,
title = "Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins",
abstract = "Tail-anchored (TA) proteins are characterised by a C-terminal transmembrane region that mediates post-translational insertion into the membrane of the endoplasmic reticulum (ER). We have investigated the requirements for membrane insertion of three TA proteins, RAMP4, Sec61beta and cytocrome b5. We show here that newly synthesised RAMP4 and Sec61beta can accumulate in a cytosolic, soluble complex with the ATPase Asna1 before insertion into ER-derived membranes. Membrane insertion of these TA proteins is stimulated by ATP, sensitive to redox conditions and blocked by alkylation of SH groups by N-ethylmaleimide (NEM). By contrast, membrane insertion of cytochrome b5 is not found to be mediated by Asna1, not stimulated by ATP and not affected by NEM or an oxidative environment. The Asna1-mediated pathway of membrane insertion of RAMP4 and Sec61beta may relate to functions of these proteins in the ER stress response.",
keywords = "Adenosine Triphosphate/metabolism, Alkylation, Animals, Arsenite Transporting ATPases/metabolism, Cytochromes b5/chemistry, Endoplasmic Reticulum/metabolism, Guinea Pigs, Humans, Intracellular Membranes/metabolism, Membrane Proteins/chemistry, Oxidation-Reduction, Oxidative Stress/physiology, Protein Structure, Tertiary/physiology, Rabbits, SEC Translocation Channels, Signal Transduction/physiology, Subcellular Fractions",
author = "Vincenzo Favaloro and Milan Spasic and Blanche Schwappach and Bernhard Dobberstein",
year = "2008",
month = jun,
day = "1",
doi = "10.1242/jcs.020321",
language = "English",
volume = "121",
pages = "1832--40",
journal = "J CELL SCI",
issn = "0021-9533",
publisher = "Company of Biologists Ltd",
number = "11",

}

RIS

TY - JOUR

T1 - Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins

AU - Favaloro, Vincenzo

AU - Spasic, Milan

AU - Schwappach, Blanche

AU - Dobberstein, Bernhard

PY - 2008/6/1

Y1 - 2008/6/1

N2 - Tail-anchored (TA) proteins are characterised by a C-terminal transmembrane region that mediates post-translational insertion into the membrane of the endoplasmic reticulum (ER). We have investigated the requirements for membrane insertion of three TA proteins, RAMP4, Sec61beta and cytocrome b5. We show here that newly synthesised RAMP4 and Sec61beta can accumulate in a cytosolic, soluble complex with the ATPase Asna1 before insertion into ER-derived membranes. Membrane insertion of these TA proteins is stimulated by ATP, sensitive to redox conditions and blocked by alkylation of SH groups by N-ethylmaleimide (NEM). By contrast, membrane insertion of cytochrome b5 is not found to be mediated by Asna1, not stimulated by ATP and not affected by NEM or an oxidative environment. The Asna1-mediated pathway of membrane insertion of RAMP4 and Sec61beta may relate to functions of these proteins in the ER stress response.

AB - Tail-anchored (TA) proteins are characterised by a C-terminal transmembrane region that mediates post-translational insertion into the membrane of the endoplasmic reticulum (ER). We have investigated the requirements for membrane insertion of three TA proteins, RAMP4, Sec61beta and cytocrome b5. We show here that newly synthesised RAMP4 and Sec61beta can accumulate in a cytosolic, soluble complex with the ATPase Asna1 before insertion into ER-derived membranes. Membrane insertion of these TA proteins is stimulated by ATP, sensitive to redox conditions and blocked by alkylation of SH groups by N-ethylmaleimide (NEM). By contrast, membrane insertion of cytochrome b5 is not found to be mediated by Asna1, not stimulated by ATP and not affected by NEM or an oxidative environment. The Asna1-mediated pathway of membrane insertion of RAMP4 and Sec61beta may relate to functions of these proteins in the ER stress response.

KW - Adenosine Triphosphate/metabolism

KW - Alkylation

KW - Animals

KW - Arsenite Transporting ATPases/metabolism

KW - Cytochromes b5/chemistry

KW - Endoplasmic Reticulum/metabolism

KW - Guinea Pigs

KW - Humans

KW - Intracellular Membranes/metabolism

KW - Membrane Proteins/chemistry

KW - Oxidation-Reduction

KW - Oxidative Stress/physiology

KW - Protein Structure, Tertiary/physiology

KW - Rabbits

KW - SEC Translocation Channels

KW - Signal Transduction/physiology

KW - Subcellular Fractions

U2 - 10.1242/jcs.020321

DO - 10.1242/jcs.020321

M3 - SCORING: Journal article

C2 - 18477612

VL - 121

SP - 1832

EP - 1840

JO - J CELL SCI

JF - J CELL SCI

SN - 0021-9533

IS - 11

ER -