PXD042259-1

PXD042259 is an original dataset announced via ProteomeXchange.

Title	K29-linked unanchored polyubiquitin chains disrupt ribosome biogenesis and direct ribosomal proteins to the Intranuclear Quality control compartment (INQ)
Description	Ribosome assembly requires precise coordination between the production and assembly of ribosomal components. Mutations in ribosomal proteins that inhibit the assembly process orribosome function are often associated with Ribosomopathies, some of which are linked to defects in proteostasis. In this study, we examine the interplay between several yeast proteostasis enzymes, including deubiquitylases (DUBs), Ubp2 and Ubp14, and E3 ligases, Ufd4 and Hul5, and we explore their roles in the regulation of the cellular levels of K29-linked unanchored polyubiquitin (polyUb) chains. Accumulating K29-linked unanchored polyUb chains associate with maturing ribosomes to disrupt their assembly, activate the Ribosome assembly stress response (RASTR), and lead to the sequestration of ribosomal proteins at the Intranuclear Quality control compartment INQ). These findings reveal the physiological relevance of INQ and provide insights into mechanisms of cellular toxicity associated with Ribosomopathies.
HostingRepository	PRIDE
AnnounceDate	2023-08-10
AnnouncementXML	Submission_2023-08-10_07:03:05.688.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD042259
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	EricBonneil
SpeciesList	scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	ubiquitinylated lysine; phosphorylated residue; monohydroxylated residue; deamidated residue
Instrument	LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2023-05-16 07:08:59	ID requested
⏵ 1	2023-08-10 07:03:06	announced
2	2023-11-14 09:04:42	announced	2023-11-14: Updated project metadata.

10.6019/PXD042259;

Suresh HG, Bonneil E, Albert B, Dominique C, Costanzo M, Pons C, David Masinas MP, Shuteriqi E, Shore D, Henras AK, Thibault P, Boone C, Andrews BJ, K29-linked unanchored polyubiquitin chains disrupt ribosome biogenesis and direct ribosomal proteins to the Intranuclear Quality control compartment (INQ). bioRxiv, ():(2023) [pubmed]

submitter keyword: Intranuclear Quality control compartment, Ribosomopathies,Unconventional K29-linked unanchored polyubiquitin chains, protein aggregation, DUB-E3 ligase interplay, ubiquitin homeostasis, ribosome assembly stress response

BrendaAndrews
contact affiliation	Univeristy Of Toronto
contact email	brenda.andrews@utoronto.ca
lab head
EricBonneil
contact affiliation	Proteomic Platform
contact email	eric.bonneil@umontreal.ca
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/2023/08/PXD042259

PRIDE project URI

• PRIDE
  1. PXD042259
     1. Label: PRIDE project
     2. Name: K29-linked unanchored polyubiquitin chains disrupt ribosome biogenesis and direct ribosomal proteins to the Intranuclear Quality control compartment (INQ)