Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins
| Autor: | Blanche Schwappach, Vincenzo Favaloro, Bernhard Dobberstein, Milan Spasic |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
Alkylation
ATPase Guinea Pigs Endoplasmic Reticulum Article chemistry.chemical_compound Adenosine Triphosphate Animals Humans biology Arsenite Transporting ATPases Endoplasmic reticulum Peripheral membrane protein Membrane Proteins Intracellular Membranes Cell Biology Protein Structure Tertiary Cell biology Oxidative Stress Cytosol Cytochromes b5 Membrane Membrane protein chemistry biology.protein Rabbits Signal transduction Oxidation-Reduction Adenosine triphosphate SEC Translocation Channels Signal Transduction Subcellular Fractions |
| Zdroj: | Journal of Cell Science. 121:1832-1840 |
| ISSN: | 1477-9137 0021-9533 |
| Popis: | 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, Sec61β and cytocrome b5. We show here that newly synthesised RAMP4 and Sec61β 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 Sec61β may relate to functions of these proteins in the ER stress response. |
| Databáze: | OpenAIRE |
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