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

Research output: Contribution to journalArticle

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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
Pages (from-to)1102-1110
Number of pages9
JournalJournal of Neurochemistry
Volume94
Issue number4
DOIs
StatePublished - Aug 1 2005

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Mitogen-Activated Protein Kinases
Chemical activation
Proteins
COS Cells
Neural Cell Adhesion Molecule L1
Mitogen-Activated Protein Kinase 3
Mitogen-Activated Protein Kinase 1
Extracellular Signal-Regulated MAP Kinases
Ran binding protein 9
Glutathione Transferase
Yeast
Neurons
Assays
Yeasts
Amino Acids
Antibodies

Keywords

  • Adhesion molecule adaptor
  • Axon extension
  • Ig superfamily

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

RanBPM is an L1-interacting protein that regulates L1-mediated mitogen-activated protein kinase activation. / Cheng, Ling; Lemmon, Sandra; Lemmon, Vance.

In: Journal of Neurochemistry, Vol. 94, No. 4, 01.08.2005, p. 1102-1110.

Research output: Contribution to journalArticle

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