The Adhesion Molecule KAL-1/anosmin-1 Regulates Neurite Branching through a SAX-7/L1CAM-EGL-15/FGFR Receptor Complex

Carlos A. Díaz-Balzac, María I. Lázaro-Peña, Gibram A. Ramos-Ortiz, Hannes E. Bülow

Research output: Contribution to journalArticle

18 Scopus citations

Abstract

Neurite branching is essential for correct assembly of neural circuits, yet it remains a poorly understood process. For example, the neural cell adhesion molecule KAL-1/anosmin-1, which is mutated in Kallmann syndrome, regulates neurite branching through mechanisms largely unknown. Here, we show that KAL-1/anosmin-1 mediates neurite branching as an autocrine co-factor with EGL-17/FGF through a receptor complex consisting of the conserved cell adhesion molecule SAX-7/L1CAM and the fibroblast growth factor receptor EGL-15/FGFR. This protein complex, which appears conserved in humans, requires the immunoglobulin (Ig) domains of SAX-7/L1CAM and the FN(III) domains of KAL-1/anosmin-1 for formation in vitro as well as function in vivo. The kinase domain of the EGL-15/FGFR is required for branching, and genetic evidence suggests that ras-mediated signaling downstream of EGL-15/FGFR is necessary to effect branching. Our studies establish a molecular pathway that regulates neurite branching during development of the nervous system.

Original languageEnglish (US)
Pages (from-to)1377-1384
Number of pages8
JournalCell Reports
Volume11
Issue number9
DOIs
StatePublished - Jun 9 2015

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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