Literature DB >> 1544474

The binding of nonmuscle caldesmon from brain to microtubules. Regulations by Ca(2+)-calmodulin and cdc2 kinase.

R Ishikawa1, O Kagami, C Hayashi, K Kohama.   

Abstract

Nonmuscle caldesmon from bovine brain bound to microtubules with a stoichiometry of five tubulin dimers to one molecule of caldesmon with values of Ka 4.5 x 10(5) 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.

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Year:  1992        PMID： 1544474     DOI： 10.1016/0014-5793(92)80099-3

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  4 in total

1.  Cytoskeletal mechanisms regulating vascular endothelial barrier function in response to acute lung injury.

Authors:  Anita Kása; Csilla Csortos; Alexander D Verin
Journal:  Tissue Barriers       Date:  2015-04-03

2.  Protein phosphatase 2A1 is the major enzyme in vertebrate cell extracts that dephosphorylates several physiological substrates for cyclin-dependent protein kinases.

Authors:  P Ferrigno; T A Langan; P Cohen
Journal:  Mol Biol Cell       Date:  1993-07       Impact factor: 4.138

3.  Smooth-muscle mitogen-activated protein (MAP) kinase: purification and characterization, and the phosphorylation of caldesmon.

Authors:  T J Childs; A S Mak
Journal:  Biochem J       Date:  1993-12-15       Impact factor: 3.857

4.  Contractile elements and myosin light chain phosphorylation in myometrial tissue from nonpregnant and pregnant women.

Authors:  R A Word; J T Stull; M L Casey; K E Kamm
Journal:  J Clin Invest       Date:  1993-07       Impact factor: 14.808
  4 in total

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