期刊
JOURNAL OF NEUROCHEMISTRY
卷 94, 期 4, 页码 1102-1110出版社
WILEY
DOI: 10.1111/j.1471-4159.2005.03254.x
关键词
adhesion molecule adaptor; axon extension; Ig superfamily
资金
- NEI NIH HHS [R01 EY005285-23, R01 EY005285] Funding Source: Medline
- NICHD NIH HHS [R01 HD039884-06, R01 HD039884] Funding Source: Medline
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.
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