Previously we reported that overexpression of MAP1B containing N-terminal 126 amino acids promoted neuronal death. Here, we identified α-, β-, and βIII-tubulins as proteins interacting with MAP1B 1-126 by two-hybrid and pull-down assays. Transfection experiments indicated that MAP1B 1-126 interacts with microtubules, but to a much lesser extent than two previously reported microtubule-binding domains. Overexpression of MAP1B 1-126 induced both neurite extension and neuronal death, suggesting that MAP1B 1-126 could be involved in neuronal degeneration and aberrant sprouting.
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http://dx.doi.org/10.1016/j.brainres.2011.11.028 | DOI Listing |
Brain Res
January 2012
Gene Expression Research Group, Research Team for Geriatic Disorders, Tokyo Metropolitan Institute of Gerontology, 35-2, Sakaecho, Itabasiku, Tokyo 173-0015, Japan.
Previously we reported that overexpression of MAP1B containing N-terminal 126 amino acids promoted neuronal death. Here, we identified α-, β-, and βIII-tubulins as proteins interacting with MAP1B 1-126 by two-hybrid and pull-down assays. Transfection experiments indicated that MAP1B 1-126 interacts with microtubules, but to a much lesser extent than two previously reported microtubule-binding domains.
View Article and Find Full Text PDFJ Biol Chem
April 2008
University of Edinburgh Cancer Centre, Cell Signalling Unit, South Crewe Road, Edinburgh, Scotland, United Kingdom.
DAPK-1 (death-activated protein kinase) has wide ranging functions in cell growth control; however, DAPK-1 interacting proteins that mediate these effects are not well defined. Protein-protein interactions are driven in part by linear interaction motifs, and combinatorial peptide libraries were used to identify peptide interfaces for the kinase domain of DAPK-1. Peptides bound to DAPK-1core kinase domain fragments had homology to the N-terminal domain of the microtubule-associated protein MAP1B.
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