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

Sun Don Kim, Jia Lie Liu, Tony Roscioli, Michael F. Buckley, Garima Yagnik, Simeon Boyd, Jinoh Kim

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1516-1521
Number of pages6
JournalFEBS Letters
Volume586
Issue number10
DOIs
StatePublished - May 21 2012

Keywords

  • Craniofacial development
  • ER export
  • FGF-signaling
  • FGFR regulation
  • Non-syndromic craniosynostosis

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

Fingerprint Dive into the research topics of 'Leucine-rich repeat, immunoglobulin-like and transmembrane domain 3 (LRIT3) is a modulator of FGFR1'. Together they form a unique fingerprint.

  • Cite this