PXD004515-1

PXD004515 is an original dataset announced via ProteomeXchange.

Title	Is transthyretin a regulator of Ubc9 SUMOylation?
Description	Ageing and mutations of transthyretin (TTR), the thyroid hormones and retinol transporting protein lead to amyloidosis by destabilizing the structure of TTR. Because protein structure is regulated through posttranslational modifications, we investigated the Small Ubiquitin-like Modifier (SUMO)ylation of TTR. We chose the widely used Ubc9 fusion-directed SUMOylation system, which is based on a fusion of the SUMOylation substrate of interest with Ubc9, a sole SUMO conjugating enzyme. Surprisingly, despite our presumptions, we found that Ubc9 fused to TTR was SUMOylated at a unique set of lysine residues. Three unknown SUMOylation sites of Ubc9—K154, K18 and K65—were revealed by mass spectrometry (MS). The previously reported SUMOylation at K49 of Ubc9 was also observed. SUMOylation of the lysine residues of TTR fused to Ubc9 was hardly detectable. However, non-fused TTR was SUMOylated via trans-SUMOylation by Ubc9 fused to TTR. Interestingly, mutating the catalytic residue of Ubc9 fused to TTR did not result in complete loss of the SUMOylation signal, suggesting that Ubc9 linked to TTR is directly cross-SUMOylated by the SUMO-activating enzyme E1. Ubc9, TTR or fusion proteins composed of TTR and Ubc9 specifically affected the global SUMOylation of cellular proteins. TTR or Ubc9 alone increased global SUMOylation, whereas TTR and Ubc9 together decreased the amount of high-molecular weight (HMW) SUMO conjugates. Our data suggest that TTR may influence the SUMOylation of Ubc9, thereby altering signalling pathways in the cell.
HostingRepository	PRIDE
AnnounceDate	2016-08-15
AnnouncementXML	Submission_2016-08-15_02:01:54.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Urszula Jankowska
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2016-07-05 05:25:44	ID requested
⏵ 1	2016-08-15 02:01:55	announced
2	2024-10-22 04:30:47	announced	2024-10-22: Updated project metadata.

Wieczorek E, K, ę, dracka-Krok S, So, ł, tys K, Jankowska U, Ho, ł, ubowicz R, Seliga J, O, ż, yhar A, Is Transthyretin a Regulator of Ubc9 SUMOylation? PLoS One, 11(8):e0160536(2016) [pubmed]

curator keyword: Biological

submitter keyword: transthyretin, Ubc9, SUMOylation, UFDS, post-translational modifications

Sylwia Kedracka-Krok
contact affiliation	Department of Physical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Krakow, Poland
contact email	sylwia.kedracka-krok@uj.edu.pl
lab head
Urszula Jankowska
contact affiliation	Jagiellonian University
contact email	urszula.jankowska@uj.edu.pl
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/2016/08/PXD004515

PRIDE project URI

• PRIDE
  1. PXD004515
     1. Label: PRIDE project
     2. Name: Is transthyretin a regulator of Ubc9 SUMOylation?