Heterotypic complex formation between subunits of microtubule-associated proteins 1A and 1B is due to interaction of conserved domains
| Autor: | Heike Stroissnigg, René Eichinger, Alžbeta Trančiková, Rainer Noiges, Friedrich Propst, Ilse Kalny |
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| Rok vydání: | 2006 |
| Předmět: |
Neuronal cytoskeleton
Microtubule-associated protein Protein subunit Plasma protein binding Biology Transfection Immunoglobulin light chain Microtubules Cell Line Conserved sequence Protein–protein interaction Structure-Activity Relationship Microtubule Animals Multimeric protein complex Molecular Biology Conserved Sequence Cell Biology Brain development Rats Protein Subunits Biochemistry Biophysics Dimerization Microtubule-Associated Proteins Protein Binding Binding domain |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1763(10):1011-1016 |
| ISSN: | 0167-4889 |
| DOI: | 10.1016/j.bbamcr.2006.08.029 |
| Popis: | The microtubule-associated proteins MAP1A and MAP1B are related but distinct multi-subunit protein complexes that consist of heavy and light chains. The predominant forms of these complexes are homotypic, i.e. they consist of a MAP1A heavy chain associated with MAP1A light chains or a MAP1B heavy chain associated with MAP1B light chains, respectively. In addition, MAP1A and MAP1B can exchange subunits and form heterotypic complexes consisting of a MAP1A heavy chain associated with MAP1B light chains which might play a role in a transition period of neuronal differentiation. Here we extend previous findings by confirming that heterotypic MAP1B heavy chain-MAP1A light chain complexes also exist in the developing murine brain. We show that these complexes form through interaction of homologous domains conserved in heavy and light chains of MAP1A and MAP1B. Likewise, conserved domains of the MAP1A and MAP1B light chains account for formation of light chain heterodimers. By yeast 2-hybrid analysis we located the light chain binding domain on the heavy chain to amino acids 211–508, thereby defining a new functional subdomain. |
| Databáze: | OpenAIRE |
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