Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins
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Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins. / Favaloro, Vincenzo; Spasic, Milan; Schwappach, Blanche; Dobberstein, Bernhard.
In: J CELL SCI, Vol. 121, No. 11, 01.06.2008, p. 1832-40.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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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 -