PXD008338-1

PXD008338 is an original dataset announced via ProteomeXchange.

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	2018-08-13
AnnouncementXML	Submission_2018-08-13_11:16:10.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

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.

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]

curator keyword: Biological

submitter keyword: Glutaminase, MAPK1, Phosphorylation, Breast Cancer, Metabolism

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

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

• PRIDE
  1. PXD008338
     1. Label: PRIDE project
     2. Name: Glutaminase C N-terminus phosphorylation decreases its enzymatic activity