Abstract:
:Clearance of misfolded proteins from the ER is central for maintenance of cellular homeostasis. This process requires coordinated recognition, ER-cytosol translocation, and finally ubiquitination-dependent proteasomal degradation. Here, we identify an ER resident seven-transmembrane protein (JAMP) that links ER chaperones, channel proteins, ubiquitin ligases, and 26S proteasome subunits, thereby optimizing degradation of misfolded proteins. Elevated JAMP expression promotes localization of proteasomes at the ER, with a concomitant effect on degradation of specific ER-resident misfolded proteins, whereas inhibiting JAMP promotes the opposite response. Correspondingly, a jamp-1 deleted Caenorhabditis elegans strain exhibits hypersensitivity to ER stress and increased UPR. Using biochemical and genetic approaches, we identify JAMP as important component for coordinated clearance of misfolded proteins from the ER.
journal_name
Mol Biol Celljournal_title
Molecular biology of the cellauthors
Tcherpakov M,Broday L,Delaunay A,Kadoya T,Khurana A,Erdjument-Bromage H,Tempst P,Qiu XB,DeMartino GN,Ronai Zdoi
10.1091/mbc.e08-08-0839subject
Has Abstractpub_date
2008-11-01 00:00:00pages
5019-28issue
11eissn
1059-1524issn
1939-4586pii
E08-08-0839journal_volume
19pub_type
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