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Leucine‐rich repeat, immunoglobulin‐like and transmembrane domain 3 (LRIT3) is a modulator of FGFR1
Author(s) -
Kim Sun-Don,
Liu Jia Lie,
Roscioli Tony,
Buckley Michael F.,
Yagnik Garima,
Boyadjiev Simeon A.,
Kim Jinoh
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.04.010
Subject(s) - fibroblast growth factor receptor , leucine rich repeat , fibroblast growth factor receptor 1 , transmembrane protein , immunoglobulin superfamily , microbiology and biotechnology , biology , transmembrane domain , immunoglobulin domain , leucine , fibroblast growth factor , receptor , biochemistry , amino acid , kinase , cell adhesion molecule
Fibroblast growth factor receptors (FGFRs) play critical roles in craniofacial and skeletal development via multiple signaling pathways including MAPK, PI3K/AKT, and PLC‐γ. FGFR‐mediated signaling is modulated by several regulators. Proteins with leucine‐rich repeat (LRR) and/or immunoglobulin (IG) superfamily domains have been suggested to interact with FGFRs. In addition, fibronectin leucine‐rich repeat transmembrane protein 3 (FLRT3) has been shown to modulate the FGFR‐mediated signaling via the fibronectin type III (FNIII) domain. Therefore proteins with LRR, IG, and FNIII are candidate regulators of the FGFRs. Here we identify leucine‐rich repeat, immunoglobulin‐like and transmembrane domain 3 (LRIT3) as a regulator of the FGFRs.