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PXD046003

PXD046003 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleSUMOylation regulates Lem2 function in centromere clustering and silencing.
DescriptionRegulation by the small modifier SUMO is heavily dependent on spatial control of enzymes that mediate the attachment and removal of SUMO on substrate proteins. Here we show that in fission yeast, delocalisation of the SUMO protease Ulp1 from the nuclear envelope results in centromeric defects that can be attributed to hyper-SUMOylation at the nuclear periphery. Unexpectedly, we find that while this localised hyper-SUMOylation impairs centromeric silencing, it can also enhance centromere clustering. Moreover, both effects are at least partially dependent on SUMOylation of the inner nuclear membrane protein Lem2. Lem2 has previously been implicated in diverse biological processes, including the promotion of both centromere clustering and silencing, but how these distinct activities are coordinated was unclear; our observations suggest a model whereby SUMOylation may serve as a regulatory switch, modulating Lem2 interactions with competing partner proteins to balance its roles in alternative pathways. Our findings also reveal a previously unappreciated role for SUMOylation in promoting centromere clustering.
HostingRepositoryPRIDE
AnnounceDate2024-10-22
AnnouncementXMLSubmission_2024-10-22_06:15:18.861.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterJoanna Strachan
SpeciesList scientific name: Schizosaccharomyces pombe 927; NCBI TaxID: 1264690;
ModificationListubiquitinylated lysine
InstrumentQ Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02023-10-09 14:27:14ID requested
12023-11-20 15:39:13announced
22024-10-22 06:15:19announced2024-10-22: Updated project metadata.
Publication List
10.1242/jcs.260868;
Strachan J, Leidecker O, Spanos C, Le Coz C, Chapman E, Arsenijevic A, Zhang H, Zhao N, Spoel SH, Bayne EH, SUMOylation regulates Lem2 function in centromere clustering and silencing. J Cell Sci, 136(23):(2023) [pubmed]
Keyword List
submitter keyword: ubiquitination, centromere, Lem2,SUMOylation,fission yeast
Contact List
Elizabeth Bayne
contact affiliationUniversity of Edinburgh
contact emailelizabeth.bayne@ed.ac.uk
lab head
Joanna Strachan
contact affiliationUniversity of Edinburgh
contact emailjo.strachan@ed.ac.uk
dataset submitter
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Dataset FTP location
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