NDLI: Control of microtubule assembly-disassembly by calcium-dependent regulator protein.

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Siderophore electrochemistry: relation to intracellular iron release mechanism.

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Detection of an early surface change during oncogenic transformation.

Control of microtubule assembly-disassembly by calcium-dependent regulator protein.

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Control of microtubule assembly-disassembly by calcium-dependent regulator protein.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Dedman, J. R. Marcum, J. M. Brinkley, B. R. Means, A. R.
Abstract	The Ca2+-dependent regulator (CDR) protein of cyclic nucleotide phosphodiesterase is a low molecular weight, acidic, Ca2+-binding protein which has been implicated in a number of Ca2+-dependent enzymatic functions. Indirect immunofluorescence has revealed that CDR is specifically associated with the chromosome-to-pole region of the mitotic apparatus during metaphase-anaphase in a pattern distinctly different from that of similar cultured cells stained with antitubulin. This characteristic localization in the mitotic half-spindle suggested a role for CDR in the control of microtubule assembly-disassembly during mitosis. Thus, CDR was examined for its effects on microtubule polymerization in vitro. It was determined that stoichiometric concentrations of CDR and a homologous Ca2+-binding protein, skeletal muscle troponin C, both inhibited and reversed microtubule assembly in a Ca2+-dependent manner. CDR-dependent inhibition of in vitro microtubule assembly occurred at physiological Ca2+ concentrations (approximately 10 micron) that, in the absence of CDR, caused only a slight reduction in polymerization. At Ca2+ concentrations in the low physiological range (less than 1 micron), no inhibition was observed. These biochemical results, together with the immunofluorescent localization of CDR in the mitotic half-spindle, provide evidence that Ca2+ is an endogenous regulator of microtubule disassembly through the activity of CDR.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	8
Volume Number	75
Language	English
Publisher	National Academy of Sciences
Publisher Date	1978-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	2',3'-Cyclic-Nucleotide Phosphodiesterases Metabolism Calmodulin Pharmacology Carrier Proteins Microtubules Phosphoric Diester Hydrolases Animals Calcium In Vitro Techniques Mitosis Parvalbumins Troponin Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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