PXD014555-1

PXD014555 is an original dataset announced via ProteomeXchange.

Title	A quantitative proteomics screen for cytoplasmic sterol binding proteins in Saccharomyces cerevisiae
Description	Cholesterol is an integral component of cellular membranes and its precise intracellular concentration and distribution is essential for maintaining cellular function. Cholesterol trafficking between cellular membranes, for example from its site of synthesis in the endoplasmic reticulum (ER) to the plasma membrane (PM) where it represents one out of every 2-3 lipids, occurs mainly by non-vesicular transport and requires carrier proteins. Known sterol transport proteins, including the oxysterol binding protein and its homologs, and StARkin proteins with sterol-binding StART domains are not physiologically essential in transporting cholesterol between the ER and PM, the route of biosynthetic sterol transport. Thus, the full complement of cytosolic sterol transport proteins (STPs) remains to be identified. Hypothesizing that STPs must first and foremost be sterol binding proteins (SBPs), we used in vivo labeling to demonstrate the presence of SBPs in yeast cytosol. Next, via an in vitro chemo-proteomic strategy involving a photo-reactive clickable cholesterol analog and quantitative mass spectrometry, we identified 342 putative SBPs. In-depth analysis of the identified proteins based on their annotated function, reported drug phenotypes (amphotericin sensitivity), reported interactions with proteins regulating lipid metabolism, gene ontology enrichment (sterol/lipid/signaling function), and conserved mammalian orthologs revealed a subset of 50 characterized and 9 uncharacterized proteins. The uncharacterized proteins are found to be involved in maintaining plasma membrane integrity based on their growth in the presence of nystatin and myriocin, drugs that target sterols and sphingolipids, respectively. The dataset reported here constitutes a comprehensive resource for functional analysis of sterol binding/transport proteins and may provide insights into novel aspects of non-vesicular sterol trafficking.
HostingRepository	PRIDE
AnnounceDate	2019-11-25
AnnouncementXML	Submission_2019-11-25_06:27:53.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Johannes Graumann
SpeciesList	scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2019-07-10 03:23:46	ID requested
⏵ 1	2019-11-25 06:27:54	announced
2	2019-11-27 06:01:03	announced	2019-11-27: Updated project metadata.
3	2021-10-29 04:31:19	announced	2021-10-29: Updated project metadata.

Chauhan N, Sere YY, Sokol AM, Graumann J, Menon AK, A PhotoClick cholesterol-based quantitative proteomics screen for cytoplasmic sterol-binding proteins in Saccharomyces cerevisiae. Yeast, 37(1):15-25(2020) [pubmed]

curator keyword: Biological

submitter keyword: LC-MS2, sterol, chemical biology

Anant K. Menon
contact affiliation	Weill Cornell Medical College, New York, NY
contact email	akm2003@med.cornell.edu
lab head
Johannes Graumann
contact affiliation	Max Planck Institute for Heart and Lung Research
contact email	johannes.graumann@mpi-bn.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/2019/11/PXD014555

PRIDE project URI

• PRIDE
  1. PXD014555
     1. Label: PRIDE project
     2. Name: A quantitative proteomics screen for cytoplasmic sterol binding proteins in Saccharomyces cerevisiae