Ca 2+-calmodulin regulated effectors of microtubule stability in neuronal tissues

• Published in: Biochimica et biophysica acta, Protein structure and molecular enzymology Vol. 1160; no. 1; pp. 113 - 119
• Main Authors: Pirollet, Fabienne, Margolis, Robert L., Job, Didier
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 10.11.1992
• Subjects: Calcium ion; Calmodulin; Microtubule; Stability; Stability; Calcium ion; Microtubule; Calmodulin
• ISSN: 0167-4838; 1879-2588
• DOI: 10.1016/0167-4838(92)90044-E

In general, microtubules are labile structures which depolymerize at low temperature and are sensitive to Ca 2+. However, in brain tissue, axonal microtubules are disassembly-resistant and can exist without attachment to a microtubule organizing center. Stable microtubules cannot be purified by usual recycling procedures and this has made the elucidation of the molecular mechanisms involved in their stabilization difficult. This paper summarizes previous work in our laboratories, aimed at the identification of brain microtubule stabilizing proteins. We present assay methods which allow the detection of microtubule stability effectors in complex extracts and in chromatographic column fractions. Applied to brain crude extracts, they result in the isolation of Ca 2+-calmodulin binding and Ca 2+-calmodulin regulated proteins. One, called STOP, appears to account for microtubule stabilization in neurons. A second protein with similar activity is myelin basic protein. Non-neuronal tissues also contain Ca 2+-calmodulin-regulated effectors which appear to differ in structure from their neuronal counterparts. Thus, in all tissues examined, microtubule stability seems to be accounted for by unique Ca 2+-calmodulin regulated proteins, showing tissue specificity.