PXD005240

PXD005240 is an original dataset announced via ProteomeXchange.

Title	Mass-Spectrometric analysis of SdeA Ubiquitin modification and Ubiquitination
Description	Conventional ubiquitination involves the ATP-dependent formation of amide bonds between the ubiquitin C-terminus and primary amines in substrate proteins. Recently, SdeA, an effector protein of pathogenic Legionella pneumophila, was shown to mediate NAD-dependent and ATP-independent ubiquitin transfer to host proteins. Yet, the molecular mechanism of this ubiquitination reaction and its relevance for cellular processes remained elusive. Here, we report the identification of a phosphodiesterase (PDE) domain in SdeA that efficiently catalyses arginine phosphoribosylation of ubiquitin via an ADP-ribose intermediate . The PDE domain also catalyzes a chemically and structurally distinct type of substrate ubiquitination by conjugating phosphoribosylated ubiquitin to serine residues of protein substrates via a phosphodiester bond. Furthermore, phosphoribosylation of ubiquitin prevents activation of E1 and E2 enzymes of the conventional ubiquitination cascade thereby diminishing numerous cellular processes including mitophagy, TNF signaling and proteasomal degradation. We propose that phosphoribosylation of ubiquitin is a potent modulator of ubiquitin functions in mammalian cells.
HostingRepository	PRIDE
AnnounceDate	2017-10-24
AnnouncementXML	Submission_2017-10-24_02:04:18.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Florian Bonn
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	omega-N-(ADP-ribosyl)-L-arginine
Instrument	Orbitrap Fusion ETD

Revision	Datetime	Status	ChangeLog Entry
0	2016-10-31 02:18:30	ID requested
1	2016-12-07 05:24:07	announced
⏵ 2	2017-10-24 02:04:19	announced	Updated project metadata.

Bhogaraju S, Kalayil S, Liu Y, Bonn F, Colby T, Matic I, Dikic I, Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination. Cell, 167(6):1636-1649.e13(2016) [pubmed]

submitter keyword: Legionella pneumophila, Orbitrap Fusion, ETD

Ivan Dikic
contact affiliation	Institute for Biochemistry II, University Hospital, Frankfurt, Germany Buchmann Institute for Molecular Life Science, Frankfurt, Germany
contact email	ivan.dikic@biochem2.de
lab head
Florian Bonn
contact affiliation	University of Frankfurt
contact email	bonn@med.uni-frankfurt.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/2016/12/PXD005240

PRIDE project URI

• PRIDE
  1. PXD005240
     1. Label: PRIDE project
     2. Name: Mass-Spectrometric analysis of SdeA Ubiquitin modification and Ubiquitination