Leucine-rich repeat, immunoglobulin-like and transmembrane domain 3 (LRIT3) is a modulator of FGFR1

FEBS Lett. 2012 May 21;586(10):1516-21. doi: 10.1016/j.febslet.2012.04.010. Epub 2012 Apr 20.


Fibroblast growth factor receptors (FGFRs) play critical roles in craniofacial and skeletal development via multiple signaling pathways including MAPK, PI3K/AKT, and PLC-?. 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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cell Line
  • DNA Primers
  • Humans
  • Immunoglobulins / metabolism*
  • Leucine / metabolism*
  • Molecular Sequence Data
  • Phospholipases / metabolism
  • Protein Kinases / metabolism
  • Receptor, Fibroblast Growth Factor, Type 1 / physiology*
  • Repetitive Sequences, Amino Acid*
  • Signal Transduction


  • DNA Primers
  • Immunoglobulins
  • Protein Kinases
  • FGFR1 protein, human
  • Receptor, Fibroblast Growth Factor, Type 1
  • Phospholipases
  • Leucine