MAP1B 1-126 interacts with tubulin isoforms and induces neurite outgrowth and neuronal death of cultured cortical neurons.

Brain Res

Gene Expression Research Group, Research Team for Geriatic Disorders, Tokyo Metropolitan Institute of Gerontology, 35-2, Sakaecho, Itabasiku, Tokyo 173-0015, Japan.

Published: January 2012

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.

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.brainres.2011.11.028DOI Listing

Publication Analysis

Top Keywords

map1b 1-126
20
neuronal death
12
1-126 interacts
8
overexpression map1b
8
map1b
6
interacts tubulin
4
tubulin isoforms
4
isoforms induces
4
induces neurite
4
neurite outgrowth
4

Similar Publications

MAP1B 1-126 interacts with tubulin isoforms and induces neurite outgrowth and neuronal death of cultured cortical neurons.

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 PDF

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.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!