PXD032366

PXD032366 is an original dataset announced via ProteomeXchange.

Title	Characterization of Xanthomonas effector protein XopL
Description	Beyond its role in intracellular degradation, autophagy is considered to play anti- and pro-microbial roles in host-microbe interactions, in both animals and plants. One of the prominent roles of anti-microbial autophagy in animals is to degrade intracellular pathogens or microbial molecules, in a process termed "xenophagy". Consequently, microbes evolved mechanisms to hijack or modulate autophagy to escape elimination. The role of xenophagy and its contribution in plant-bacteria interactions still remain unknown. Here, we provide evidence that NBR1/Joka2-dependent selective autophagy functions in plant defence by degrading the bacterial type-III effector (T3E) XopL from Xanthomonas campestris pv. vesicatoria (Xcv). We further describe how XopL associates with the autophagy machinery, undergoes self-ubiquitination and in planta ubiquitination triggering its degradation by the NBR1/Joka2 selective autophagy pathway. However, Xcv is also able to suppress autophagy in a T3E-dependent manner by utilizing the same T3E XopL that interacts and degrades the autophagy component SH3P2 via its E3 ligase activity. Through the degradation of SH3P2 and inhibition of autophagy, XopL is able to escape its own degradation to promote pathogenicity of Xcv. Together, we reveal a novel phenomenon how the NBR1/Joka2 contributes to anti-microbial autophagy that we termed "effectorphagy". We provide a unique mechanism how a T3E undergoes self-modification to act as a bait to trap host cellular degradation machineries.
HostingRepository	PRIDE
AnnounceDate	2022-08-12
AnnouncementXML	Submission_2022-08-12_00:14:46.624.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Mirita Franz-Wachtel
SpeciesList	scientific name: Nicotiana benthamiana; NCBI TaxID: 4100;
ModificationList	ubiquitinylated lysine; phosphorylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2022-03-17 09:27:55	ID requested
⏵ 1	2022-08-12 00:14:47	announced

Leong JX, Raffeiner M, Spinti D, Langin G, Franz-Wachtel M, Guzman AR, Kim JG, Pandey P, Minina AE, Macek B, Hafr, é, n A, Bozkurt TO, Mudgett MB, B, ö, rnke F, Hofius D, Ü, st, ü, n S, A bacterial effector counteracts host autophagy by promoting degradation of an autophagy component. EMBO J, 41(13):e110352(2022) [pubmed]

submitter keyword: LC-MSMS, bacterial effectors, plants

Suayb Üstün
contact affiliation	Faculty of Biology & Biotechnology Ruhr-University Bochum D-44780 Bochum Germany
contact email	suayb.uestuen@rub.de
lab head
Mirita Franz-Wachtel
contact affiliation	Proteome Center Tuebingen
contact email	mirita.franz@uni-tuebingen.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/2022/08/PXD032366

PRIDE project URI

• PRIDE
  1. PXD032366
     1. Label: PRIDE project
     2. Name: Characterization of Xanthomonas effector protein XopL