PXD004256

PXD004256 is an original dataset announced via ProteomeXchange.

Title	in vitro ubiquitination by E3 ligase Cbl-b
Description	Fungal infections claim an estimated 1.5 million lives every year. Mechanisms that protect from fungal infections are still elusive. Recognition of fungal pathogens relies on C-type lectin receptors (CLR) and their downstream signaling kinase SYK. Here we report that the E3-ubiquitin-ligase CBL-B controls proximal C-type lectin receptor signaling in macrophages and dendritic cells. We show that CBL-B associates with SYK and ubiquitinates SYK, Dectin-1, and Dectin-2 upon fungal recognition. Functionally, CBL-B deficiency results in increased inflammasome activation, enhanced reactive oxygen species production, and increased fungal killing. Genetic deletion of Cblb protects mice from morbidity caused by cutaneous infection and markedly improves survival upon a lethal systemic infection with Candida albicans. Based on these findings, we engineered a cell-permeable CBL-B inhibitory peptide that protects mice from lethal C. albicans infections. We thus describe a key role for Cblb in the regulation of innate anti-fungal immunity and establish a novel paradigm for the treatment of fungal sepsis.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:29:51.011.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Richard Imre
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	methylthiolated residue; ubiquitination signature dipeptidyl lysine; phosphorylated residue; deaminated residue; acetylated residue; monohydroxylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2016-05-31 03:31:31	ID requested
1	2016-06-17 08:21:05	announced
⏵ 2	2024-10-22 04:29:51	announced	2024-10-22: Updated project metadata.

Dataset with its publication pending

curator keyword: Biological, Biomedical

submitter keyword: LC-MS, Cbl-b,ubiquitin linkage

Josef Penninger
contact affiliation	Institute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), 1030 Vienna, Austria
contact email	Josef.Penninger@imba.oeaw.ac.at
lab head
Richard Imre
contact affiliation	IMBA - Institute of Molecular Biotechnology
contact email	imre@imp.ac.at
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/2016/06/PXD004256

PRIDE project URI

• PRIDE
  1. PXD004256
     1. Label: PRIDE project
     2. Name: in vitro ubiquitination by E3 ligase Cbl-b