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

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.
Sun-Don Kim 1,  Jia Lie Liu,  Tony Roscioli,  Michael F Buckley,  Garima Yagnik,  Simeon A Boyadjiev,  Jinoh Kim
Affiliations

Affiliation

  • 1 Section of Genetics, Department of Pediatrics, University of California Davis Medical Center, Sacramento, CA 95817, USA.
PMID: 22673519 DOI: 10.1016/j.febslet.2012.04.010
Abstract

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.

Figures