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PXD018517-1

PXD018517 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleThe RNF185/Membralin ubiquitin ligase complex is a new ERAD branch involved in the degradation of a distinct subset of integral membrane proteins.
DescriptionThe endoplasmic reticulum-associated degradation (ERAD) pathway is responsible for ubiquitin-mediated quality control of secretory and ER-resident proteins. In the present study, two short-lived ER integral membrane model proteins were used to screen a genome-wide CRISPR-Cas9 library, resulting in the identification of a new ERAD branch consisting of the RNF185/Membralin ubiquitin ligase complex. Biochemical and affinity pull-down studies followed by mass spectrometry revealed that the ubiquitin-like domain containing proteins TMUB-1 and -2 are also part of the core complex being specifically enriched by RNF185/Membralin but not by other known ERAD factors like HRD1. Genetic studies showed that the RNF185/Membralin complex control the degradation of endogenous integral membrane proteins, including TMUB2 itself and CYP51A1 from which the initial recombinant model protein was derived.
HostingRepositoryPRIDE
AnnounceDate2024-10-07
AnnouncementXMLSubmission_2024-10-07_10:39:21.691.xml
DigitalObjectIdentifierhttps://dx.doi.org/10.6019/PXD018517
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterPedro Carvalho
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListOxidation; Acetyl; acetylated residue; iodoacetamide derivatized residue
InstrumentQ Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02020-04-14 01:53:32ID requested
12024-10-07 10:39:22announced
Publication List
10.1016/j.molcel.2020.07.009;
10.6019/PXD018517;
Keyword List
submitter keyword: Endoplasmic reticulum-associated degradation (ERAD)
E3 ligase RNF185
Membralin
TMEM259
TMUB1
TMUB2
ubiquitin
Contact List
Pedro Carvalho
contact affiliationSir William Dunn School of Pathology University of Oxford United Kingdom
contact emailpedro.carvalho@path.ox.ac.uk
lab head
Pedro Carvalho
contact affiliationUniversity of Oxford
contact emailpedro.carvalho@path.ox.ac.uk
dataset submitter
Full Dataset Link List
Dataset FTP location
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