PXD010167

PXD010167 is an original dataset announced via ProteomeXchange.

Title	A quantitative proteomic view of cofilin phosphorylation and its modulation using the LIM kinase inhibitor Pyr1
Description	LIM kinases are located at a strategic crossroad, downstream of several signaling pathways and upstream of effectors such as microtubules and the actin cytoskeleton.. Cofilin is the only LIM kinases substrate that is well described to date, and its phosphorylation on serine 3 by LIM Kinases controls cofilin actin-severing activity. Consequently, LIM Kinases inhibition leads to actin cytoskeleton disorganization and blockade of cell motility, which makes this strategy attractive in anticancer strategies. We have used proteomic approaches to investigate quantitatively and in detail the phosphorylation status of cofilin in myeloid tumor cell lines of murine and human origin. Our results show that under standard conditions, only a relatively small fraction (10 to 30% depending on the cell line) of cofilin is phosphorylated (including serine 3 phosphorylation). In addition, after a pharmacological inhibition of LIM kinases, a residual cofilin phosphorylation is observed on serine 3. Interestingly, this 2D gel based proteomic study identified new phosphorylation sites on cofilin, such as threonine 63, tyrosine 82 and serine 108.
HostingRepository	PRIDE
AnnounceDate	2018-12-19
AnnouncementXML	Submission_2018-12-21_01:36:13.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Hélène Diemer
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	phosphorylated residue; acetylated residue
Instrument	TripleTOF 5600

Revision	Datetime	Status	ChangeLog Entry
0	2018-06-19 06:09:34	ID requested
1	2018-12-19 04:43:57	announced
⏵ 2	2018-12-21 01:36:15	announced	Updated publication reference for PubMed record(s): 30550596.

Prudent R, Demoncheaux N, Diemer H, Collin-Faure V, Kapur R, Paublant F, Lafanech, è, re L, Cianf, é, rani S, Rabilloud T, A quantitative proteomic analysis of cofilin phosphorylation in myeloid cells and its modulation using the LIM kinase inhibitor Pyr1. PLoS One, 13(12):e0208979(2018) [pubmed]

curator keyword: Biological

submitter keyword: Cofilin, Human, Mouse, Phosphorylation, 2D gel, LC-MS/MS

Sarah Cianférani
contact affiliation	Laboratoire de Spectrométrie de Masse BioOrganique (LSMBO), Université de Strasbourg, CNRS, IPHC UMR 7178, 67087 Strasbourg Cedex 2, France
contact email	sarah.cianferani@unistra.fr
lab head
Hélène Diemer
contact affiliation	LSMBO
contact email	hdiemer@unistra.fr
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/2018/12/PXD010167

PRIDE project URI

• PRIDE
  1. PXD010167
     1. Label: PRIDE project
     2. Name: A quantitative proteomic view of cofilin phosphorylation and its modulation using the LIM kinase inhibitor Pyr1