The binding of nonmuscle caldesmon from brain to microtubules Regulations by Ca2+‐calmodulin and cdc2 kinase
- 2 March 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 299 (1) , 54-56
- https://doi.org/10.1016/0014-5793(92)80099-3
Abstract
Nonmuscle caldesmon from bovine brain bound to microtubules with a stoichiometry of five tubulin dimers to one molecule of caldesmon with values of K A 4.5×105 M−1. The binding of caldesmon to microtubules was inhibited in the presence of Ca2+ and calmodulin. The phosphorylation of caldesmon by cdc2 kinase also eliminated the microtubule-binding activity. These results suggest that caldesmon may play a physiological role in the functions of microtubules.Keywords
This publication has 22 references indexed in Scilit:
- Phosphorylation of non-muscle caldesmon by p34cdc2 kinase during mitosisNature, 1991
- Mitosis-specific phosphorylation causes 83K non-muscle caldesmon to dissociate from microfilamentsNature, 1990
- Universal control mechanism regulating onset of M-phaseNature, 1990
- Purification and Characterization of 83 kDa Nonmuscle Caldesmon from Cultured Rat Cells: Changes in Its Expression upon L 6 MyogenesisPublished by Springer Nature ,1988
- Evidence for interaction between smooth muscle tropomyosin and caldesmonFEBS Letters, 1987
- Purification and characterization of caldesmon77: a calmodulin-binding protein that interacts with actin filaments from bovine adrenal medulla.Proceedings of the National Academy of Sciences, 1985
- Evidence for an involvement of actin in the positioning and motility of centrosomes.The Journal of cell biology, 1985
- Microtubule-associated proteins (MAPs) and the organization of actin filaments in vitro.The Journal of cell biology, 1981
- Nucleotide and corresponding amino acid sequences encoded by α and β tubulin mRNAsNature, 1981
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979