PXD059792-1

PXD059792 is an original dataset announced via ProteomeXchange.

Title	The EMC acts as a chaperone to labile transmembrane domains
Description	Structure formation of membrane proteins is error-prone and thus requires chaperones that oversee this essential process in cell biology. The ER membrane protein complex (EMC) is well-defined as a transmembrane domain (TMD) integrase. In this study, we characterize an additional chaperone function of the EMC. We use interactomics and systematic studies with model proteins to comprehensively define client features for this EMC chaperone mode. Based on this data, we develop a machine learning tool for client prediction. Mechanistically, our study reveals that the EMC engages TMDs via its EMC1 subunit and modulates their orientation within the lipid bilayer. Productive TMD assembly reduces binding to the EMC chaperone site. Taken together, our study provides detailed insights into an EMC chaperone function, further establishing the role of the EMC as a multifunctional molecular machine in membrane protein biogenesis.
HostingRepository	PRIDE
AnnounceDate	2025-08-25
AnnouncementXML	Submission_2025-08-24_16:37:00.456.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Barbara Steigenberger
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	No PTMs are included in the dataset
Instrument	timsTOF Pro

Revision	Datetime	Status	ChangeLog Entry
0	2025-01-14 14:13:31	ID requested
⏵ 1	2025-08-24 16:37:01	announced

10.1038/s41467-025-62109-x;

Klose CJ, Meighen-Berger KM, Kulke M, Parr M, Steigenberger B, Zacharias M, Frishman D, Feige MJ, The EMC acts as a chaperone for membrane proteins. Nat Commun, 16(1):7097(2025) [pubmed]

submitter keyword: membrane proteins, endoplasmic reticulum, chaperone, protein folding

Matthias J. Feige
contact affiliation	Cellular Protein Biochemistry Lab Technical University of Munich School of Natural Sciences Department of Bioscience
contact email	matthias.feige@tum.de
lab head
Barbara Steigenberger
contact affiliation	MPI of Biochemistry
contact email	steigenberger@biochem.mpg.de
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/08/PXD059792

PRIDE project URI

• PRIDE
  1. PXD059792
     1. Label: PRIDE project
     2. Name: The EMC acts as a chaperone to labile transmembrane domains