Open AccessA TRCky TA protein delivery service snubs the UPS
Author(s) -
Alexander J. McQuown,
Dvir Reif,
Vladimir Denic
Publication year - 2021
Publication title -
the journal of cell biology/the journal of cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.414
H-Index - 380
eISSN - 1540-8140
pISSN - 0021-9525
DOI - 10.1083/jcb.202103196
Subject(s) - biology , proteasome , microbiology and biotechnology , ubiquitin , chaperone (clinical) , hek 293 cells , protein degradation , membrane protein , membrane , biochemistry , gene , pathology , medicine
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.