Tyrosine phosphorylation profiling in FGF-2 stimulated human embryonic stem cells.

Bibliographic Details
Title: Tyrosine phosphorylation profiling in FGF-2 stimulated human embryonic stem cells.
Authors: Vanessa M Y Ding, Paul J Boersema, Leong Yan Foong, Christian Preisinger, Geoffrey Koh, Subaashini Natarajan, Dong-Yup Lee, Jos Boekhorst, Berend Snel, Simone Lemeer, Albert J R Heck, Andre Choo
Source: PLoS ONE, Vol 6, Iss 3, p e17538 (2011)
Publisher Information: Public Library of Science (PLoS), 2011.
Publication Year: 2011
Collection: LCC:Medicine
LCC:Science
Subject Terms: Medicine, Science
More Details: The role of fibroblast growth factor-2 (FGF-2) in maintaining undifferentiated human embryonic stem cells (hESC) was investigated using a targeted phosphoproteomics approach to specifically profile tyrosine phosphorylation events following FGF-2 stimulation. A cumulative total number of 735 unique tyrosine phosphorylation sites on 430 proteins were identified, by far the largest inventory to date for hESC. Early signaling events in FGF-2 stimulated hESC were quantitatively monitored using stable isotope dimethyl labeling, resulting in temporal tyrosine phosphorylation profiles of 316 unique phosphotyrosine peptides originating from 188 proteins. Apart from the rapid activation of all four FGF receptors, trans-activation of several other receptor tyrosine kinases (RTKs) was observed as well as induced tyrosine phosphorylation of downstream proteins such as PI3-K, MAPK and several Src family members. Both PI3-K and MAPK have been linked to hESC maintenance through FGF-2 mediated signaling. The observed activation of the Src kinase family members by FGF-2 and loss of pluripotent marker expression post Src kinase inhibition may point to the regulation of cytoskeletal and actin depending processes to maintain undifferentiated hESC.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 1932-6203
Relation: https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21437283/pdf/?tool=EBI; https://doaj.org/toc/1932-6203
DOI: 10.1371/journal.pone.0017538
Access URL: https://doaj.org/article/adbbe8a9de054032b918e4b6a0ff1945
Accession Number: edsdoj.bbe8a9de054032b918e4b6a0ff1945
Database: Directory of Open Access Journals
More Details
ISSN:19326203
DOI:10.1371/journal.pone.0017538
Published in:PLoS ONE
Language:English