RanBPM is an L1-interacting protein that regulates L1-mediated mitogen-activated protein kinase activation

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Abstract

A yeast two-hybrid screen using the last 28 amino acids of the cytoplasmic domain of the neural cell adhesion molecule L1 identified RanBPM as an L1-interacting protein. RanBPM associates with L1 in vivo and the N-terminal region of RanBPM (N-RanBPM), containing the SPRY domain, is sufficient for the interaction with L1 in a glutathione S-transferase pull-down assay. L1 antibody patching dramatically changes the subcellular localization of N-RanBPM in transfected COS cells. Overexpression of N-RanBPM in COS cells reduces L1-triggered extracellular signal-regulated kinase 1/2 activation by 50% and overexpression of N-RanBPM in primary neurons inhibits L1-mediated neurite outgrowth and branching. These data suggest that RanBPM is an adaptor protein that links L1 to the extracellular signal-regulated kinase/MAPK pathway.

Original languageEnglish (US)
Pages (from-to)1102-1110
Number of pages9
JournalJournal of neurochemistry
Volume94
Issue number4
DOIs
StatePublished - Aug 2005

Keywords

  • Adhesion molecule adaptor
  • Axon extension
  • Ig superfamily

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

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