PXD034237-1

PXD034237 is an original dataset announced via ProteomeXchange.

Title	Analysis of DVL3 polyglutamylation using Q-TOF
Description	Polyglutamylation is a reversible post-translational modification initially discovered on tubulin. In eukaryotes, polyglutamylation is catalyzed by enzymes from the tubulin tyrosine ligase-like (TTLL) family, which show substrate and reaction specificities that are so far mostly explored on tubulin. By contrast, little is known on the mechanism and significance of TTLL-mediated modification of non-tubulin substrates. Here, we found that TTLL11 generates a previously unknown type of polyglutamylation by adding glutamate residues to the carboxy-terminus of a substrate protein. TTLL11 efficiently polyglutamylates the signaling protein disheveled 3 (DVL3), thereby changing the interactome of DVL3, as well as its capacity to undergo liquid-liquid phase separation (LLPS). Both carboxyterminal polyglutamylation and the resulting reduction in LLPS capacity of DVL3 were reverted by the deglutamylating enzyme CCP6, which demonstrates the causal relationship between TTLL11-mediated polyglutamylation and LLPS. We thus discovered a novel type of posttranslational modification catalyzed by a TTLL enzyme, which significantly broadens the range of proteins that can be modified by polyglutamylation, and provide first evidence that polyglutamylation can act as a regulator of protein LLPS.
HostingRepository	PRIDE
AnnounceDate	2024-09-30
AnnouncementXML	Submission_2024-09-30_07:16:32.235.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD034237
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	David Potesil
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	No PTMs are included in the dataset
Instrument	impact II

Revision	Datetime	Status	ChangeLog Entry
0	2022-06-01 03:53:37	ID requested
⏵ 1	2024-09-30 07:16:32	announced

10.6019/PXD034237;

10.1038/S44318-024-00254-7;

submitter keyword: TTLL11, WNT signaling, LC-MS, polyglutamylation,DVL3, interactome

Zbynek Zdrahal
contact affiliation	Proteomics Core Facility and Research Group Proteomics, CEITEC-MU, Masaryk University, Brno, Czech Republic
contact email	zdrahal@sci.muni.cz
lab head
David Potesil
contact affiliation	Proteomics Core Facility and Research Group Proteomics CEITEC-MU Masaryk University Brno, Czech Republic
contact email	david.potesil@ceitec.muni.cz
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/2024/09/PXD034237

PRIDE project URI

• PRIDE
  1. PXD034237
     1. Label: PRIDE project
     2. Name: Analysis of DVL3 polyglutamylation using Q-TOF