Regulatory functions of calmodulin.

Calmodulin is a Ca2+ binding protein present in all eukaryotic cells that serves as the primary intracellular receptor for Ca2+. This 148 amino acid protein is involved in activation of more than 20 enzymes which mediate a wide variety of physiological processes. Many of these enzymes are inhibited in an intramolecular manner and the Ca(2+)-calmodulin complex relieves this inhibition. Calmodulin is essential for life as disruption of the gene in genetically tractable organisms is lethal. This protein plays important regulatory roles in cell proliferation and is required at multiple points in the cell cycle. The mechanism of enzyme activation by calmodulin and its importance in cell growth regulation are reviewed.

[1]  L. V. Van Eldik,et al.  Use of DNA sequence and mutant analyses and antisense oligodeoxynucleotides to examine the molecular basis of nonmuscle myosin light chain kinase autoinhibition, calmodulin recognition, and activity , 1990, The Journal of cell biology.

[2]  A. Means,et al.  Myosin light chain kinase structure function analysis using bacterial expression. , 1989, The Journal of biological chemistry.

[3]  Charles E. Bugg,et al.  Three-dimensional structure of calmodulin , 1985, Nature.

[4]  A. Means,et al.  Autoregulation of enzymes by pseudosubstrate prototopes: myosin light chain kinase. , 1988, Science.

[5]  B. Mitchell,et al.  Calcium, magnesium, and growth control in the WI-38 human fibroblast cell , 1979, The Journal of cell biology.

[6]  T. Vanaman,et al.  Calcium and calmodulin in cell growth and transformation. , 1984, Biochimica et biophysica acta.

[7]  E. Krebs,et al.  Isolation of the cDNA encoding rat skeletal muscle myosin light chain kinase. Sequence and tissue distribution. , 1988, Journal of Biological Chemistry.

[8]  M. Ikebe,et al.  Location of the inhibitory region of smooth muscle myosin light chain kinase. , 1989, The Journal of biological chemistry.

[9]  M. James,et al.  Model for the interaction of amphiphilic helices with troponin C and calmodulin , 1990, Proteins.

[10]  F G Prendergast,et al.  Calmodulin binding domains: characterization of a phosphorylation and calmodulin binding site from myosin light chain kinase. , 1986, Biochemistry.

[11]  A. Means,et al.  Changes in calmodulin and its mrna accompany reentry of quiescent (G0) cells into the cell cycle , 1984, Cell.

[12]  T. Davis,et al.  Isolation of the yeast calmodulin gene: Calmodulin is an essential protein , 1986, Cell.

[13]  A. Zetterberg,et al.  Kinetic analysis of regulatory events in G1 leading to proliferation or quiescence of Swiss 3T3 cells. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[14]  A. Means,et al.  Chimeric calmodulin-cardiac troponin C proteins differentially activate calmodulin target enzymes. , 1990, The Journal of biological chemistry.

[15]  H. Schulman,et al.  Ca2+/calmodulin kinase is activated by the phosphatidylinositol signaling pathway and becomes Ca2(+)-independent in PC12 cells. , 1990, The Journal of biological chemistry.

[16]  A. Means,et al.  Chicken calmodulin promoter activity in proliferating and differentiated cells. , 1989, Molecular endocrinology.

[17]  P. Bodine,et al.  Related effects of calcium and serum on the G1 phase of the human WI38 fibroblast , 1980, Journal of cellular physiology.

[18]  A. Edelman,et al.  Rabbit skeletal muscle myosin light chain kinase. The calmodulin binding domain as a potential active site-directed inhibitory domain. , 1987, The Journal of biological chemistry.

[19]  H. Hidaka,et al.  Calmodulin and cell proliferation. , 1982, Biochemical and biophysical research communications.

[20]  A. Edelman,et al.  Identification of the calmodulin-binding domain of skeletal muscle myosin light chain kinase. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[21]  A. Means,et al.  Calmodulin activation of target enzymes. Consequences of deletions in the central helix. , 1990, The Journal of biological chemistry.

[22]  R. Waterston,et al.  Sequence of an unusually large protein implicated in regulation of myosin activity in C. elegans , 1989, Nature.

[23]  H. Schulman,et al.  Multifunctional Ca2+/calmodulin-dependent protein kinase is necessary for nuclear envelope breakdown , 1990, The Journal of cell biology.

[24]  D. Newton,et al.  CAPP‐calmodulin: A potent competitive inhibitor of calmodulin actions , 1984, FEBS letters.

[25]  A. Means,et al.  Proteolysis of smooth muscle myosin light chain kinase. Formation of inactive and calmodulin-independent fragments. , 1987, The Journal of biological chemistry.

[26]  M. James,et al.  Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution , 1985, Nature.

[27]  F. Maxfield,et al.  Local cytoplasmic calcium gradients in living mitotic cells , 1985, Nature.

[28]  C. Foster,et al.  Potent peptide inhibitors of smooth muscle myosin light chain kinase: mapping of the pseudosubstrate and calmodulin binding domains. , 1990, Archives of biochemistry and biophysics.

[29]  A. Means,et al.  Calmodulin and the cell cycle: Involvement in regulation of cell-cycle progression , 1982, Cell.

[30]  T. Davis,et al.  Vertebrate and yeast calmodulin, despite significant sequence divergence, are functionally interchangeable. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[31]  A. Means,et al.  NMR studies of a complex of deuterated calmodulin with melittin. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[32]  M. Groudine,et al.  Levels of c-myc oncogene mRNA are invariant throughout the cell cycle , 1985, Nature.

[33]  R. Kretsinger,et al.  Structure and evolution of calcium-modulated proteins. , 1980, CRC critical reviews in biochemistry.

[34]  A. Means,et al.  Calmodulin is required for cell‐cycle progression during G1 and mitosis. , 1989, The EMBO journal.

[35]  R. Waring,et al.  Characterization of an inducible expression system in Aspergillus nidulans using alcA and tubulin-coding genes. , 1989, Gene.

[36]  T. Soderling.  Protein kinases. Regulation by autoinhibitory domains. , 1990, The Journal of biological chemistry.

[37]  A. Means,et al.  Tubulin and calmodulin. Effects of microtubule and microfilament inhibitors on localization in the mitotic apparatus , 1979, The Journal of cell biology.

[38]  N. Morris,et al.  Kinetics of the nuclear division cycle of Aspergillus nidulans , 1983, Journal of bacteriology.

[39]  M. James,et al.  Common structural framework of the two Ca2+/Mg2+ binding loops of troponin C and other Ca2+ binding proteins. , 1985, Biochemistry.

[40]  J. Doonan,et al.  The bimG gene of Aspergillus nidulans, required for completion of anaphase, encodes a homolog of mammalian phosphoprotein phosphatase 1 , 1989, Cell.

[41]  T. Davis,et al.  Can calmodulin function without binding calcium? , 1991, Cell.

[42]  D. Beach,et al.  The cdc2 kinase is a nuclear protein that is essential for mitosis in mammalian cells , 1989, Cell.

[43]  W. Jackson,et al.  Detection of the membrane-calcium distribution during mitosis in Haemanthus endosperm with chlorotetracycline , 1980, The Journal of cell biology.

[44]  H. Hidaka,et al.  Transmembrane Ca2+ signaling and a new class of inhibitors. , 1987, Methods in enzymology.

[45]  J Moult,et al.  A model for the Ca2+-induced conformational transition of troponin C. A trigger for muscle contraction. , 1986, The Journal of biological chemistry.

[46]  William F. DeGrado,et al.  How calmodulin binds its targets: sequence independent recognition of amphiphilic α-helices , 1990 .

[47]  A. Means,et al.  Calcium-dependent regulator protein: localization in mitotic apparatus of eukaryotic cells. , 1978, Proceedings of the National Academy of Sciences of the United States of America.

[48]  R. Steinhardt,et al.  Intracellular free calcium rise triggers nuclear envelope breakdown in the sea urchin embryo , 1988, Nature.

[49]  G. May.  The highly divergent beta-tubulins of Aspergillus nidulans are functionally interchangeable , 1989, The Journal of cell biology.

[50]  D. Blumenthal,et al.  Amino acid sequence of rabbit skeletal muscle myosin light chain kinase. , 1986, Biochemistry.

[51]  D. Blumenthal,et al.  Activation of skeletal muscle myosin light chain kinase by calcium(2+) and calmodulin. , 1980, Biochemistry.

[52]  G. Mayr,et al.  Skeletal muscle myosin light chain kinase , 1983, FEBS letters.

[53]  S. Hirono,et al.  Quantitative structure-activity relationships for calmodulin inhibitors. , 1990, Chemical & pharmaceutical bulletin.

[54]  J. Spudich,et al.  Dictyostelium myosin light chain kinase. Purification and characterization. , 1990, The Journal of biological chemistry.

[55]  A. Means,et al.  Calmodulin is involved in regulation of cell proliferation. , 1987, The EMBO journal.

[56]  J. Trewhella,et al.  Comparison of the crystal and solution structures of calmodulin and troponin C. , 1988, Biochemistry.

[57]  T. Takeda,et al.  Analysis and in vivo disruption of the gene coding for calmodulin in Schizosaccharomyces pombe. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[58]  M. Whitaker,et al.  Translational control of InsP3-induced chromatin condensation during the early cell cycles of sea urchin embryos , 1988, Nature.

[59]  D. Storm,et al.  Calcium binding to complexes of calmodulin and calmodulin binding proteins. , 1985, Biochemistry.

[60]  T. Gibson,et al.  A regular pattern of two types of 100-residue motif in the sequence of titin , 1990, Nature.

[61]  Marc W. Kirschner,et al.  Unpolymerized tubulin modulates the level of tubulin mRNAs , 1981, Cell.

[62]  A. Means,et al.  The presence of parvalbumin in a nonmuscle cell line attenuates progression through mitosis. , 1989, Molecular endocrinology.

[63]  D. Hartshorne,et al.  Identification in turkey gizzard of an acidic protein related to the C-terminal portion of smooth muscle myosin light chain kinase. , 1989, The Journal of biological chemistry.

[64]  Roger Y. Tsien,et al.  Changes of free calcium levels with stages of the cell division cycle , 1985, Nature.

[65]  B. Weiss.  Techniques for measuring the interaction of drugs with calmodulin. , 1983, Methods in enzymology.

[66]  A. Means,et al.  Domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNA. , 1986, Biochemistry.

[67]  J. Doonan,et al.  Spindle formation and chromatin condensation in cells blocked at interphase by mutation of a negative cell cycle control gene , 1988, Cell.

[68]  V. Guerriero,et al.  Hormonal regulation of a chicken oviduct messenger ribonucleic acid that shares a common domain with gizzard myosin light chain kinase. , 1987, Molecular endocrinology.

[69]  H. Schulman,et al.  Multifunctional Ca2+/calmodulin-dependent protein kinase made Ca2+ independent for functional studies. , 1990, Biochemistry.

[70]  A. Means,et al.  The calmodulin binding domain of chicken smooth muscle myosin light chain kinase contains a pseudosubstrate sequence. , 1987, The Journal of biological chemistry.

[71]  P. Walker,et al.  THE ROLES OF CALCIUM AND CYCLIC AMP IN CELL PROLIFERATION , 1980, Annals of the New York Academy of Sciences.

[72]  A. Means,et al.  Characterization and expression of the unique calmodulin gene of Aspergillus nidulans. , 1990, The Journal of biological chemistry.

[73]  G. Saunders,et al.  Mitosis-specific monoclonal antibody MPM-2 inhibits Xenopus oocyte maturation and depletes maturation-promoting activity. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[74]  A. Means,et al.  Regulatory and structural motifs of chicken gizzard myosin light chain kinase. , 1990, Proceedings of the National Academy of Sciences of the United States of America.