PXD008338 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | Glutaminase C N-terminus phosphorylation decreases its enzymatic activity |
| Description | The gene GLS generates the phosphate activated glutaminase C (GAC) isoform by alternative splicing. GAC, compared to the other isoform, kidney-type glutaminase (KGA), has been characterized as more active and particularly important for cancer cell growth. Very little is known about post-translational modifications regulating GAC function. Hereby we describe the identification of a phosphorylation on the serine 95, located at the GLS N-terminus, a domain shared by both isoforms. A GAC phosphomimetic mutant (S95D) ectopically expressed in breast cancer cells presented decreased enzymatic activity, and its expression impacted on cell’s glutamine uptake, glutamate release and intracellular glutamate levels (compared to expressing wild type GAC) without changing GAC sub-cellular localization. Curiously, replacing S95 by an alanine in the ectopically expressed GAC (S95A) increased cell proliferation and migration. Taken together, these results reveal that GAC is post-translationally regulated by phosphorylation, which impacts on cancer phenotype. |
| HostingRepository | PRIDE |
| AnnounceDate | 2024-10-22 |
| AnnouncementXML | Submission_2024-10-22_04:42:33.605.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Adriana Franco Paes Leme |
| SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
| ModificationList | phosphorylated residue |
| Instrument | LTQ Orbitrap Velos |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
|---|
| 0 | 2017-11-30 01:19:23 | ID requested | |
| 1 | 2018-08-13 11:16:11 | announced | |
| ⏵ 2 | 2024-10-22 04:42:41 | announced | 2024-10-22: Updated project metadata. |
Publication List
| Ascen, ç, ã, o CFR, Nagampalli RSK, Islam Z, Pinheiro MP, Menezes Dos Reis L, Pauletti BA, de Guzzi Cassago CA, Granato DC, Paes Leme AF, Dias SMG, N-terminal phosphorylation of glutaminase C decreases its enzymatic activity and cancer cell migration. Biochimie, 154():69-76(2018) [pubmed] |
| 10.1016/j.biochi.2018.07.022; |
Keyword List
| curator keyword: Biological |
| submitter keyword: Metabolism, MAPK1, Breast Cancer,Glutaminase, Phosphorylation |
Contact List
| adriana franco paes leme |
|---|
| contact affiliation | Brazilian Biosciences National Laboratory (LNBio), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, Sao Paulo, Brazil, Zip Code 13083-970 |
| contact email | adriana.paesleme@lnbio.cnpem.br |
| lab head | |
| Adriana Franco Paes Leme |
|---|
| contact affiliation | CNPEM |
| contact email | adriana.paesleme@lnbio.cnpem.br |
| dataset submitter | |
Full Dataset Link List
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/2018/08/PXD008338 |
| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD008338
- Label: PRIDE project
- Name: Glutaminase C N-terminus phosphorylation decreases its enzymatic activity
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