Phosphorylation of microtubule-associated proteins by a Ca2+/calmodulin- dependent protein kinase

doi:10.1083/jcb.99.1.11

This Article

	Full Text (PDF, 1222K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Schulman, H
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Schulman, H


Social Bookmarking

	What's this?

ARTICLES

Phosphorylation of microtubule-associated proteins by a Ca2+/calmodulin- dependent protein kinase

H Schulman

In an earlier study I demonstrated that rat brain cytosol contains a Ca2+/calmodulin-dependent protein kinase activity that phosphorylates microtubule-associated protein 2 (MAP-2) but not MAP-1. Comparison of sites of phosphate incorporated in MAP-2 catalyzed by the Ca2+/calmodulin-dependent kinase activity and the cyclic AMP-dependent protein kinase activity in cytosolic extracts revealed distinct sites of phosphorylation (Schulman, H., 1984, Mol. Cell. Biol., 4:1175-1178; abstract by me and J.A. Kuret and K.H. Spitzer [1983, Fed. Proc., 42:2250]. I have now used MAP-2 as a substrate to purify the Ca2+/calmodulin-dependent protein kinase responsible for MAP-2 phosphorylation. The brain appears to contain a single predominant Ca2+/calmodulin-dependent protein kinase that phosphorylates MAP-2. The enzyme was purified to apparent homogeneity by column chromatography using DEAE-cellulose, phosphocellulose, hydroxylapatite, Sepharose 6B, and a calmodulin-Sepharose affinity column. The 580,000-dalton holoenzyme consists of 51,000- and 60,000-dalton subunits. The purified enzyme phosphorylates MAP-2 at the same "sites" that are phosphorylated in cytosolic extracts and thus has the same specificity as the activity present in cytosol. Analysis of phosphorylated MAP-2.1 and MAP-2.2, the two components of MAP-2, suggests considerable homology in their phosphorylated domains.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Flynn, M. P., Maizels, E. T., Karlsson, A. B., McAvoy, T., Ahn, J.-H., Nairn, A. C., Hunzicker-Dunn, M. (2008). Luteinizing Hormone Receptor Activation in Ovarian Granulosa Cells Promotes Protein Kinase A-Dependent Dephosphorylation of Microtubule-Associated Protein 2D. Mol. Endocrinol. 22: 1695-1710 [Abstract] [Full Text]
Vest, R. S., Davies, K. D., O'Leary, H., Port, J. D., Bayer, K. U. (2007). Dual Mechanism of a Natural CaMKII Inhibitor. Mol. Biol. Cell 18: 5024-5033 [Abstract] [Full Text]
Yuen, E. Y., Jiang, Q., Chen, P., Gu, Z., Feng, J., Yan, Z. (2005). Serotonin 5-HT1A Receptors Regulate NMDA Receptor Channels through a Microtubule-Dependent Mechanism. J. Neurosci. 25: 5488-5501 [Abstract] [Full Text]
Chen, J. Y.-F., Chang, Y.-L., Yu, Y.-C., Chao, C.-C., Kao, H.-W., Wu, C.-T., Lin, W.-C., Ko, J.-Y., Jou, Y.-S. (2004). Specific induction of the high-molecular-weight microtubule-associated protein 2 (hmw-MAP2) by betel quid extract in cultured oral keratinocytes: clinical implications in betel quid-associated oral squamous cell carcinoma (OSCC). Carcinogenesis 25: 269-276 [Abstract] [Full Text]
Ahluwalia, B., Ahmad, S., Adeyiga, O., Wesley, B., Rajguru, S. (2000). LOW LEVELS OF ETHANOL STIMULATE AND HIGH LEVELS DECREASE PHOSPHORYLATION IN MICROTUBULE-ASSOCIATED PROTEINS IN RAT BRAIN: AN IN VITRO STUDY. Alcohol Alcohol 35: 452-457 [Abstract] [Full Text]
Brocke, L., Chiang, L. W., Wagner, P. D., Schulman, H. (1999). Functional Implications of the Subunit Composition of Neuronal CaM Kinase II. J. Biol. Chem. 274: 22713-22722 [Abstract] [Full Text]
Philpot, B. D., Lim, J. H., Halpain, S., Brunjes, P. C. (1997). Experience-Dependent Modifications in MAP2 Phosphorylation in Rat Olfactory Bulb. J. Neurosci. 17: 9596-9604 [Abstract] [Full Text]
Krueger, K. A., Bhatt, H., Landt, M., Easom, R. A. (1997). Calcium-stimulated Phosphorylation of MAP-2 in Pancreatic beta TC3-cells Is Mediated by Ca2+/Calmodulin-dependent Kinase II. J. Biol. Chem. 272: 27464-27469 [Abstract] [Full Text]
Quinlan, E. M., Halpain, S. (1996). Emergence of Activity-Dependent, Bidirectional Control of Microtubule-Associated Protein MAP2 Phosphorylation during Postnatal Development. J. Neurosci. 16: 7627-7637 [Abstract] [Full Text]
Hain, J�r., Onoue, H., Mayrleitner, M., Fleischer, S., Schindler, H. (1995). Phosphorylation Modulates the Function of the Calcium Release Channel of Sarcoplasmic Reticulum from Cardiac Muscle. J. Biol. Chem. 270: 2074-2081 [Abstract] [Full Text]
Meyer, T., Hanson, P. I., Stryer, L., Schulman, H. (1992). Calmodulin Trapping by Calcium-Calmodulin-Dependent Protein Kinase. Science 256: 1199-1202 [Abstract]
Jones, E.G., Benson, D.L., Hendry, S.H.C., Isackson, P.J. (1990). Activity-dependent Regulation of Gene Expression in Adult Monkey Visual Cortex. Cold Spring Harb Symp Quant Biol 55: 481-490 [Abstract]
Poenie, M, Alderton, J, Steinhardt, R, Tsien, R (1986). Calcium rises abruptly and briefly throughout the cell at the onset of anaphase. Science 233: 886-889 [Abstract]