PXD046003

PXD046003 is an original dataset announced via ProteomeXchange.

Title	SUMOylation regulates Lem2 function in centromere clustering and silencing.
Description	Regulation 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.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_06:15:18.861.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Joanna Strachan
SpeciesList	scientific name: Schizosaccharomyces pombe 927; NCBI TaxID: 1264690;
ModificationList	ubiquitinylated lysine
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2023-10-09 14:27:14	ID requested
1	2023-11-20 15:39:13	announced
⏵ 2	2024-10-22 06:15:19	announced	2024-10-22: Updated project metadata.

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]

submitter keyword: ubiquitination, centromere, Lem2,SUMOylation,fission yeast

Elizabeth Bayne
contact affiliation	University of Edinburgh
contact email	elizabeth.bayne@ed.ac.uk
lab head
Joanna Strachan
contact affiliation	University of Edinburgh
contact email	jo.strachan@ed.ac.uk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD046003
     1. Label: PRIDE project
     2. Name: SUMOylation regulates Lem2 function in centromere clustering and silencing.