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

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 t...

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Autores principales:	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
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/adbbe8a9de054032b918e4b6a0ff1945
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spelling	oai:doaj.org-article:adbbe8a9de054032b918e4b6a0ff19452021-11-18T06:57:12ZTyrosine phosphorylation profiling in FGF-2 stimulated human embryonic stem cells.1932-620310.1371/journal.pone.0017538https://doaj.org/article/adbbe8a9de054032b918e4b6a0ff19452011-03-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21437283/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The 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.Vanessa M Y DingPaul J BoersemaLeong Yan FoongChristian PreisingerGeoffrey KohSubaashini NatarajanDong-Yup LeeJos BoekhorstBerend SnelSimone LemeerAlbert J R HeckAndre ChooPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 3, p e17538 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q 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 Tyrosine phosphorylation profiling in FGF-2 stimulated human embryonic stem cells.
description	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.
format	article
author	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
author_facet	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
author_sort	Vanessa M Y Ding
title	Tyrosine phosphorylation profiling in FGF-2 stimulated human embryonic stem cells.
title_short	Tyrosine phosphorylation profiling in FGF-2 stimulated human embryonic stem cells.
title_full	Tyrosine phosphorylation profiling in FGF-2 stimulated human embryonic stem cells.
title_fullStr	Tyrosine phosphorylation profiling in FGF-2 stimulated human embryonic stem cells.
title_full_unstemmed	Tyrosine phosphorylation profiling in FGF-2 stimulated human embryonic stem cells.
title_sort	tyrosine phosphorylation profiling in fgf-2 stimulated human embryonic stem cells.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/adbbe8a9de054032b918e4b6a0ff1945
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Tyrosine phosphorylation profiling in FGF-2 stimulated human embryonic stem cells.

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