PXD051014

PXD051014 is an original dataset announced via ProteomeXchange.

Title	Profiling the LAM family of contact-site tethers provides mechanistic insights into their regulation and function
Description	Membrane contact sites are molecular bridges between organelles that are sustained by tethering proteins and enable organelle communication. The endoplasmic reticulum (ER) membrane harbors many distinct families of tether proteins that enable the formation of contacts with all other organelles. One such example is the LAM (Lipid transfer protein At Membrane contact sites) family, composed of six members. All six LAM proteins share the presence of a sterol transfer domain and a transmembrane segment that anchors them to the ER. However, the six proteins are divided into three homologous pairs each unique in their molecular architecture and localization to different ER subdomains. What determines the distinct localization of the different LAMs and which specific roles they carry out in each contact are still open questions. To address these, we utilized a proximity labeling approach to profile the interaction landscape of the entire family. Focusing on unique interactors we could support a role for Lam5 at the ER-mitochondria contact site. Capturing shared interactors of multiple LAMs explains how Lam1/3 and Lam2/4 paralogous pairs could be associated specifically with the plasma membrane. Overall, our work provides new insights into the regulation and function of the pan-ER contact LAM family proteins. More globally it demonstrates how proximity labeling can help identify the shared or unique functions of paralogous proteins.
HostingRepository	PRIDE
AnnounceDate	2025-05-06
AnnouncementXML	Submission_2025-05-06_13:42:14.671.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Christof Lenz
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2024-03-27 05:46:16	ID requested
⏵ 1	2025-05-06 13:42:15	announced

10.1177/25152564251321770;

Fenech EJ, Kupervaser M, Boshnakovska A, Ravid S, Castro IG, Asraf Y, Callegari S, Lenz C, Urlaub H, Rehling P, Schuldiner M, Profiling the LAM Family of Contact Site Tethers Provides Insights into Their Regulation and Function. Contact (Thousand Oaks), 8():25152564251321770(2025) [pubmed]

submitter keyword: membrane contact sites

endoplasmic reticulum

LAM protein family

proximity labelling

ABOLISH

Christof Lenz
contact affiliation	Core Facility Proteomics, Department of Clinical Chemistry, University Medical Center Goettingen, Germany
contact email	christof.lenz@med.uni-goettingen.de
lab head
Christof Lenz
contact affiliation	Max Planck Institute for Biophysical Chemistry
contact email	christof.lenz@mpibpc.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/2025/05/PXD051014

PRIDE project URI

• PRIDE
  1. PXD051014
     1. Label: PRIDE project
     2. Name: Profiling the LAM family of contact-site tethers provides mechanistic insights into their regulation and function