A TRCky TA protein delivery service snubs the UPS.
| Autor: | McQuown AJ; Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA., Reif D; Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA., Denic V; Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA. |
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| Jazyk: | angličtina |
| Zdroj: | The Journal of cell biology [J Cell Biol] 2021 May 03; Vol. 220 (5). |
| DOI: | 10.1083/jcb.202103196 |
| Abstrakt: | In mammals, tail-anchored (TA) proteins that are posttranslationally captured by the chaperone SGTA are triaged by the BAG6 complex into one of two fates: handoff to an ER targeting factor for membrane insertion or polyubiquitination for destruction by the proteasome. In this issue, Culver and Mariappan (2021. J. Cell Biol.https://doi.org/10.1083/jcb.202004086) show that a fraction of newly synthesized TA proteins is polyubiquitinated in HEK293 cells independently of the BAG6 complex yet evades proteasomal degradation by undergoing deubiquitination en route to becoming stably inserted into the ER membrane. (© 2021 McQuown et al.) |
| Databáze: | MEDLINE |
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