NDLI: Separation of endogenous calmodulin- and cAMP-dependent kinases from microtubule preparations.

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Separation of endogenous calmodulin- and cAMP-dependent kinases from microtubule preparations.

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Separation of endogenous calmodulin- and cAMP-dependent kinases from microtubule preparations.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Goldenring, J. R. Buckholz, T. M. Larson, R. E. Delorenzo, R. J. Vallano, M. L.
Abstract	Both cAMP- and calmodulin-dependent kinases are proposed regulators of microtubule function by means of their ability to phosphorylate microtubule-associated protein 2(MAP 2). A cAMP-dependent kinase/MAP 2 complex is endogenous to microtubules. In this report, we demonstrate that an endogenous calmodulin-dependent kinase that phosphorylates MAP 2 as a major substrate is also present in microtubules prepared under conditions that preserve kinase activity. This enzyme is identical to a calmodulin-dependent kinase purified previously from rat brain cytosol. A fraction containing calmodulin-dependent kinase and MAP 2 was separated from the cAMP-dependent kinase/MAP 2 complex by gel filtration chromatography of microtubule protein in high ionic strength buffer. All of the recovered calmodulin-dependent kinase activity in microtubules eluted in a single protein peak. The specific activity of the enzyme for MAP 2 was enriched 31-fold in this fraction compared to cytosol. Two-dimensional tryptic phosphopeptide mapping revealed that the endogenous cAMP- and calmodulin-dependent kinases phosphorylated distinct sites on MAP 2. These data demonstrate that both kinases are present in microtubule preparations and that they may differentially regulate MAP 2 function by phosphorylating separate sites on MAP 2.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	10
Volume Number	82
Language	English
Publisher	National Academy of Sciences
Publisher Date	1985-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Calmodulin Metabolism Microtubule-Associated Proteins Microtubules Enzymology Protein Kinases Isolation & Purification Animals Brain Macromolecular Substances Peptide Fragments Phosphoproteins Phosphorylation Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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