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@article{1395567,
author = {Bálek, Lukáš and Němec, Pavel and Konik, P. and Bosáková, Michaela and Vařecha, Miroslav and Gudernová, Iva and Medalová, Jiřina and Krakow, Deborah and Krejčí, Pavel},
article_location = {New York},
article_number = {JAN 2018},
doi = {http://dx.doi.org/10.1016/j.cellsig.2017.10.003},
keywords = {FGFR3; Fibroblast growth factor; interactome; receptor tyrosine kinase; signal transduction},
language = {eng},
issn = {0898-6568},
journal = {Cellular Signalling},
title = {Proteomic analyses of signalling complexes associated with receptor tyrosine kinase identify novel members of fibroblast growth factor receptor 3 interactome},
volume = {42},
year = {2018}
}
TY - JOUR
ID - 1395567
AU - Bálek, Lukáš - Němec, Pavel - Konik, P. - Bosáková, Michaela - Vařecha, Miroslav - Gudernová, Iva - Medalová, Jiřina - Krakow, Deborah - Krejčí, Pavel
PY - 2018
TI - Proteomic analyses of signalling complexes associated with receptor tyrosine kinase identify novel members of fibroblast growth factor receptor 3 interactome
JF - Cellular Signalling
VL - 42
IS - JAN 2018
SP - 144-154
EP - 144-154
PB - Elsevier Science
SN - 08986568
KW - FGFR3
KW - Fibroblast growth factor
KW - interactome
KW - receptor tyrosine kinase
KW - signal transduction
N2 - Receptor tyrosine kinases (RTKs) form multiprotein complexes that initiate and propagate intracellular signals and determine the RTK-specific signalling patterns. Unravelling the full complexity of protein interactions within the RTK-associated complexes is essential for understanding of RTK functions, yet it remains an understudied area of cell biology. We describe a comprehensive approach to characterize RTK interactome. A single tag immunoprecipitation and phosphotyrosine protein isolation followed by mass-spectrometry was used to identify proteins interacting with fibroblast growth factor receptor 3 (FGFR3). A total of 32 experiments were carried out in two different cell types and identified 66 proteins out of which only 20 (30.3%) proteins were already known FGFR interactors. Using co-immunoprecipitations, we validated FGFR3 interaction with adapter protein STAM1, transcriptional regulator SHOX2, translation elongation factor eEF1A1, serine/threonine kinases ICK, MAK and CCRK, and inositol phosphatase SHIP2. We show that unappreciated signalling mediators exist for well-studied RTKs, such as FGFR3, and may be identified via proteomic approaches described here. These approaches are easily adaptable to other RTKs, enabling identification of novel signalling mediators for majority of the known human RTKs.
ER -
BÁLEK, Lukáš, Pavel NĚMEC, P. KONIK, Michaela BOSÁKOVÁ, Miroslav VAŘECHA, Iva GUDERNOVÁ, Jiřina MEDALOVÁ, Deborah KRAKOW a Pavel KREJČÍ. Proteomic analyses of signalling complexes associated with receptor tyrosine kinase identify novel members of fibroblast growth factor receptor 3 interactome. \textit{Cellular Signalling}. New York: Elsevier Science, 2018, roč.~42, JAN 2018, s.~144-154. ISSN~0898-6568. Dostupné z: https://dx.doi.org/10.1016/j.cellsig.2017.10.003.
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