Apocalmodulin

Physiological Reviews

Volumn 79, Issue 3, 1999, Pages 661-682

  Jurado, Luis A ^a   Chockalingam, Priya Sethu ^a   Jarrett, Harry W ^a  

^a UNIVERSITY OF TENNESSEE HEALTH SCIENCE CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; APOCALMODULIN; CALCIUM ION; CALMODULIN; CALMODULIN DERIVATIVE; ION CHANNEL; MEMBRANE PROTEIN; PHOSPHOPROTEIN; PROTEIN KINASE; UNCLASSIFIED DRUG;

CALCIUM BINDING; CALCIUM CELL LEVEL; COMPLEX FORMATION; CYTOSKELETON; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN STRUCTURE; RECEPTOR INTRINSIC ACTIVITY; REVIEW; SECOND MESSENGER; SEQUENCE ANALYSIS;

EID: 0032779780     PISSN: 00319333     EISSN: None     Source Type: Journal    
DOI: 10.1152/physrev.1999.79.3.661     Document Type: Review

References (157)

1. ALEXANDER, K. A., B. M. CIMLER, K. E. MEIER, AND D. R. STORM. Regulation of calmodulin binding to P-57. J. Biol. Chem. 262: 6108-6113, 1987.
2. ANAGLI, J., F. HOFMANN, M. QUADRONI, T. VORHERR, AND E. CARAFOLI. The calmodulin-binding domain of the inducible (macrophage) nitric oxide synthase. Eur. J. Biochem. 233: 701-708, 1995.
3. 2+-calmodulin binds to the carboxyl-terminal domain of dystrophin. J. Biol. Chem. 271: 6605-6610, 1996.
4. ANDREASEN, T. J., C. W. LUETJE, W. HEIDEMAN, AND D. R. STORM. Purification of a novel calmodulin binding protein from bovine cerebral cortex membranes. Biochemistry 22: 4615-4618, 1983.
5. APEL, E. D., M. F. BYFORD, D. AU, K. A. WALSH, AND D. R. STORM. Identification of the protein kinase C phosphorylation site in neuromodulin. Biochemistry 29: 2330-2335, 1990.
6. ARAZI, T., G. BAUM, W. A. SNEDDEN, B. J. SHELP, AND H. FROMM. Molecular and biochemical analysis of calmodulin interactions with the calmodulin-binding domain of plant glutamate decarboxylase. Plant Physiol. 108: 551-561, 1995.
7. BABU, Y. S., J. S. SACK, T. J. GREENHOUGH, C. E. BUGG, A. R. MEANS, AND W. J. COOK. Three-dimensional structure of calmodulin. Nature 315: 37-40, 1985.
8. BACHS, O., L. LANINI, J. SERRATOSA, M. J. COLL, R. BASTOS, R. ALIGUE, E. RIUS, AND E. CARAFOLI. Calmodulin-binding proteins in the nuclei of quiescent and proliferatively activated rat liver cells. J. Biol. Chem. 265: 18595-18600, 1990.
9. BAHLER, M., R. KROSCHEWSKI, H. E. STOFFLER, AND T. BEHRMANN. Rat myr 4 defines a novel subclass of myosin: identification, distribution, localization, and mapping of calmodulin-binding sites with differential calcium sensitivity. J. Cell Biol. 126: 375-389, 1994.
10. BAUDIER, J., J. C. DELOULME, A. V. DORSSELAER, D. BLACK, AND H. W. D. MATTHES. Purification and characterization of a brain-specific protein kinase C substrate, neurogranin (p17). J. Biol. Chem. 266: 229-237, 1991.
11. BAUM, G., Y. CHEN, T. ARAZI, H. TAKATSUJI, AND H. FROMM. A plant glutamate decarboxylase containing a calmodulin binding domain. Cloning, sequence, and functional analysis. J. Biol. Chem. 268: 19610-19617, 1993.
12. 2+/calmodulin-dependent protein kinase determined by molecular cloning. Proc. Natl. Acad. Sci. USA 84: 1794-1798, 1987.
13. BERRIDGE, M. J. Inositol trisphosphate and diacylglycerol: two interacting second messengers. Annu. Rev. Biochem. 56: 159-193, 1987.
14. BRAAM, J., AND R. W. DAVIS. Rain-, wind-, and touch-induced expression of calmodulin and calmodulin-related genes in Arabidopsis. Cell 60: 357-364, 1990.
15. BRILL, S., S. LI, C. W. LYMAN, D. M. CHURCH, J. J. WASMUTH, L. WEISBACH, A. BERNARDS, AND A. SNIJDERS. The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases. Mol. Cell. Biol. 16: 4869-4878, 1996.
16. BROCKERHOFF, S. E., AND T. N. DAVIS. Calmodulin concentrates at regions of cell growth in Saccharomyces cerevisiae. J. Cell Biol. 118: 619-629, 1992.
17. BROCKERHOFF, S. E., R. C. STEVENS, AND T. N. DAVIS. The unconventional myosin, Myo2p, is a calmodulin target at sites of cell growth in Saccharomyces cerevisiae. J. Cell Biol. 124: 315-323, 1994.
18. 2+, calmodulin, and phosphorylase kinase. J. Biol. Chem. 258: 14733-14739, 1983.
19. CARAFOLI, E., AND C. B. KLEE. Preface: new developments in the calmodulin field. Cell Calcium 13: 353-354, 1992.
20. CHABEREK, S., AND A. E. MARTELL. Metal Buffers. New York: Wiley, 1959, p. 1-616.
21. CHAFOULEAS, J. G., W. E. BOLTON, H. HIDAKA, A. E. BOYD III, AND A. R. MEANS. Calmodulin and the cell cycle: involvement in regulation of cell-cycle progression. Cell 28: 41-50, 1982.
22. CHAPMAN, E. R., D. AU, K. A. ALEXANDER, T. A. NICOLSON, AND D. R. STORM. Characterization of the calmodulin binding domain of neuromodulin. J. Biol. Chem. 266: 207-213, 1991.
23. CHENEY, R. E., AND M. S. MOOSEKER. Unconventional myosins. Curr. Opin. Cell Biol. 4: 27-35, 1992.
24. CHEUNG, W. Y. Cyclic 3′,5′-nucleotide phosphodiesterase. Demonstration of an activator. Biochem. Biophys. Res. Commun. 38: 533-538, 1970.
25. CIMLER, B. M., T. J. ANDREASEN, K. I. ANDREASEN, AND D. R. STORM. P-57 is a neural specific calmodulin-binding protein. J. Biol. Chem. 260: 10784-10788, 1985.
26. COHEN, P. The role of calcium ions, calmodulin and troponin in the regulation of phosphorylase kinase from rabbit skeletal muscle. Eur. J. Biochem. 111: 563-574, 1980.
27. COHEN, P. Calmodulin. Amsterdam: Elsevier Science, 1988.
28. 2+-dependent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase. FEBS Lett. 92: 287-293, 1978.
29. COX, J. A. Interactive properties of calmodulin. Biochem. J. 249: 621-629, 1988.
30. CRIVICI, A., AND M. IKURA. Molecular and structural basis of target recognition by calmodulin. Annu. Rev. Biophys. Biomol. Struct. 24: 85-116, 1995.
31. CYERT, M. S., R. KUNISAWA, D. KAIM, AND J. THORNER. Yeast has homologs (CNA1 and CNA2 gene products) of mammalian calcineurin, a calmodulin-regulated phosphoprotein phosphatase. Proc. Natl. Acad. Sci. USA 88: 7376-7380, 1991.
32. DASGUPTA, M., T. HONEYCUTT, AND D. K. BLUMENTHAL. The γ-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin. J. Biol. Chem. 264: 17156-17163, 1989.
33. DA SILVA, A. C., AND F. C. REINACH. Calcium binding induces conformational changes in muscle regulatory proteins. Trends Biochem. Sci. 16: 53-57, 1991.
34. DAVIS, T. N. A temperature-sensitive calmodulin mutant loses viability during mitosis. J. Cell Biol. 118: 607-617, 1992.
35. DAVIS, T. N., AND J. THORNER. Vertebrate and yeast calmodulin, despite significant sequence divergence, are functionally interchangeable. Proc. Natl. Acad. Sci. USA 86: 7909-7913, 1989.
36. DAVIS, T. N., M. S. URDEA, F. R. MASIARZ, AND J. THORNER. Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell 47: 423-431, 1986.
37. DINSMORE, J. H., AND R. D. SLOBODA. Calcium and calmodulin-dependent phosphorylation of a 62 kd protein induces microtubule depolymerization in sea urchin mitotic apparatus. Cell 53: 769-780, 1988.
38. EDELMAN, A. M., K. TAKIO, D. K. BLUMENTHAL, K. A. WALSH, K. TITANI, AND E. G. KREBS. Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase. J. Biol. Chem. 260: 11275-11285, 1985.
39. ERVASTI, J. M., AND K. P. CAMPBELL. Membrane organization of the dystrophin-glycoprotein complex. Cell 66: 1121-1131, 1991.
40. ESPREAFICO, E. M., R. E. CHENEY, M. MATTEOLI, A. A. C. NASCIMENTO, P. V. DECAMILLI, R. E. LARSON, AND M. S. MOOSEKER. Primary structure and cellular localization of chicken brain myosin-V (p 190), an unconventional myosin with calmodulin light chains. J. Cell Biol. 119: 1541-1557, 1992.
41. EVAIN, D., C. KLEE, AND W. B. ANDERSON. Chinese hamster ovary cell population density affect intracellular concentrations of the calcium-dependent regulator and the ability of regulator to inhibit adenylate cyclase activity. Proc. Natl. Acad. Sci. USA 76: 3962-3966, 1979.
42. FAUST, F., M. SLISZ, AND H. W. JARRETT. Calmodulin is labeled at lysine 148 by a chemically reactive phenothiazine. J. Biol. Chem. 262: 1938-1941, 1987.
43. FRIEDBERG, F. Species comparison of calmodulin sequences. Protein Seq. Data Anal. 3: 335-337, 1990.
44. FROEHNER, S. C. Peripheral proteins of postsynaptic membranes from Torpedo electric organ identified with monoclonal antibodies. J. Cell Biol. 99: 88-96, 1984.
45. GARCIA, A., E. COUDRIER, J. CARBONI, J. ANDERSON, J. VANDEKERKHOVE, M. MOOSEKER, D. LOUVARD, AND M. ARPIN. Partial deduced sequence of the 110-kD calmodulin complex of the avian intestinal microvillus show that this mechanoenzyme is a member of the myosin I family. J. Cell Biol. 109: 2895-2903, 1989.
46. GEE, S. H., R. MADHAVAN, S. R. LEVINSON, J. H. CALDWELL, R. SEALOCK, AND S. C. FROEHNER. Interactions of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated proteins. J. Neurosci. 18: 128-137, 1998.
47. GEISER, J. R., H. A. SUNDBERG, B. H. CHANG, E. G. MULLER, AND T. N. DAVIS. The essential mitotic target of calmodulin is the 110-kilodalton component of the spindle pole body in Saccharomyces cerevisiae. Mol. Cell. Biol. 13: 7913-7924, 1993.
48. GEISER, J. R., D. VAN TUINEN, S. E. BROCKERHOFF, M. M. NEFF, AND T. N. DAVIS. Can calmodulin function without binding calcium? Cell 65: 949-959, 1991.
49. GENTILE, F., L. G. KNIPLING, D. L. SACKETT, AND J. WOLFF. Invasive adenylate cyclase of Bordetella pertussis. Physical, catalytic, and toxic properties. J. Biol. Chem. 265: 10686-10692, 1990.
50. GLASER, P., A. ELMAOGLOU-LAZARIDOU, E. KRIN, D. LADANT, O. BARZU, AND A. DANCHIN. Identification of residues essential for catalysis and binding of calmodulin in Bordetella pertussis adenylate cyclase by site directed mutagenesis. EMBO J. 8: 967-972, 1989.
51. 2+)ATPase. Biochem. Biophys. Res. Commun. 77: 1203-1209, 1977.
52. GREENLEE, D. V., T. J. ANDREASEN, AND D. R. STORM. Calcium-independent stimulation of Bortedella pertussis adenylate cyclase. Biochemistry 21: 2759-2764, 1982.
53. HAIECH, J., C. B. KLEE, AND J. G. DEMAILLE. Effects of cations on affinity of calmodulin for calcium: ordered binding of calcium ions allows the specific activation of calmodulin-stimulated enzymes. Biochemistry 20: 3890-3897, 1981.
54. HARPER, J. F., W. Y. CHEUNG, R. W. WALLACE, H.-L. HUANG, S. N. LEVINE, AND A. L. STEINER. Localization of calmodulin in rat tissues. Proc. Natl. Acad. Sci. USA 77: 366-370, 1980.
55. HARRIS, E., P. YASWEN, AND J. THORNER. Gain-of-function mutations in a human calmodulin-like protein identify residues critical for calmodulin action in yeast. Mol. Gen. Genet. 247: 137-147, 1995.
56. +-ATPase assembly. Genetics 141: 833-844, 1995.
57. HOUDUSSE, A., AND C. COHEN. Target sequence recognition by the calmodulin superfamily: implications from light chain binding to the regulatory domain of scallop myosin. Proc. Natl. Acad. Sci. USA 92: 10644-10647, 1995.
58. 2+-free calmodulin binding to unconventional myosins reveals how calmodulin acts as a regulatory switch. Structure 4: 1475-1490, 1996.
59. IKURA, M., G. M. CLORE, A. M. GRONENBORN, G. ZHU, C. B. KLEE, AND A. BAX. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256: 632-638, 1992.
60. 1-Syntrophin has distinct binding sites for actin and calmodulin. FEBS Lett. 423: 173-177, 1998.
61. JAMES, P., T. VORHERR, AND E. CARAFOLI. Calmodulin-binding domains: just two faced or multi-faceted? Trends Biochem. Sci. 20: 38-42, 1995.
62. JARRETT, H. W., C. J. BROWN, C. C. BLACK, AND M. J. CORMIER. Evidence that calmodulin is in the chloroplast of peas and serves a regulatory role in photosynthesis. J. Biol. Chem. 257: 13795-13804, 1982.
63. JARRETT, H. W., AND J. L. FOSTER. Alternate binding of actin and calmodulin to multiple sites on dystrophin. J. Biol. Chem. 270: 5578-5586, 1995.
64. 2+-ATPase activator from human erythrocytes: its similarity to the activator of 3′:5′-cyclic nucleotide phosphodiesterase. Biochem. Biophys. Res. Commun. 77: 1210-1216, 1977.
65. KAKIUCHI, S., AND R. YAMAZAKI. Calcium dependent phosphodiesterase activity and its activating factor (PAF) from brain studies on cyclic 3′,5′-nucleotide phosphodiesterase (3). Biochem. Biophys. Res. Commun. 41: 1104-1110, 1970.
66. KAKIUCHI, S., S. YASUDA, R. YAMAZAKI, Y. TESHIMA, K. KANDA, R. KAKIUCHI, AND K. SOBUE. Quantitative determinations of calmodulin in the supernatant and particulate fractions of mammalian tissues. J. Biochem. 92: 1041-1048, 1982.
67. 2+ in mitotic progression of Swiss 3T3 fibroblasts. J. Cell Biol. 111: 183-196, 1990.
68. KEITH, C. H. Effect of microinjected calcium-calmodulin on mitosis in PtK2 cells. Cell Motil. Cytoskeleton 7: 1-9, 1987.
69. KELLER, C. H., B. B. OLWIN, D. C. LAPORTE, AND D. R. STORM. Determination of the free-energy coupling for binding of calcium ions and troponin I to calmodulin. Biochemistry 21: 156-162, 1982.
70. KINK, J. A., M. E. MALEY, R. R. PRESTON, K. Y. LING, M. A. WALLEN- FRIEDMAN, Y. AIMI, AND C. KUNG. Mutations in Paramecium calmodulin indicate functional differences between the C-terminal and N-terminal lobes in-vivo. Cell 62: 165-174, 1990.
71. KOENIG, M., A. P. MONACO, AND L. M. KUNKEL. The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein. Cell 53: 219-226, 1988.
72. KREBS, E. G., AND J. A. BEAVO. Phosphorylation-dephosphorylation of enzymes. Annu. Rev. Biochem. 48: 923-959, 1979.
73. KRETSINGER, R. H. Structure and evolution of calcium-modulated proteins. CRC Crit. Rev. Biochem. 8: 119-174, 1980.
74. KRETSINGER, R. H., S. E. RUDNICK, AND L. J. WEISSMAN. Crystal structure of calmodulin. J. Inorg. Biochem. 28: 289-302, 1986.
75. KUBLER, E., F. SCHIMMOLLER, AND H. REIZMAN. Calcium-independent calmodulin requirement for endocytosis in yeast. EMBO J. 13: 5539-5546, 1994.
76. LADANT, D. Interaction of Bordetella pertussis adenylate cyclase with calmodulin. Identification of two separate calmodulin-binding domains. J. Biol. Chem. 263: 2612-2618, 1988.
77. LIN, C. T., J. R. DEDMAN, B. R. BRINKLEY, AND A. R. MEANS. Localization of calmodulin in rat cerebellum by immunoelectron microscopy. J. Cell Biol. 85: 473-480, 1980.
78. LIN, Y. M. Calmodulin. Mol. Cell. Biochem. 45: 101-112, 1982.
79. LING, V., W. A. SNEDDEN, B. J. SHELP, AND S. M. ASSMANN. Analysis of a soluble calmodulin binding protein from fava bean roots: identification of glutamate decarboxylase as a calmodulin-activated enzyme. Plant Cell 6: 1135-1143, 1994.
80. LIU, J., J. D. FARMER, W. S. LANE, J. FRIEDMAN, I. WEISSMAN, AND S. L SCHREIBER. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 66: 807-815, 1991.
81. LIU, Y. C., AND D. R. STORM. Regulation of free calmodulin levels by neuromodulin: neuron growth and regeneration. Trends Pharmacol. Sci. 11: 107-111, 1990.
82. 2+/calmodulin-dependent protein kinase in Saccharomyces cerevisiae. FEBS Lett. 219: 249-253, 1987.
83. 2/M progression in Aspergillus nidulans. J. Cell Biol. 121: 621-630, 1993.
84. LUAN, Y., I. MATSUURA, M. YAZAWA, T. NAKAMURA, AND K. YAGI. Yeast calmodulin: structural and functional differences compared with vertebrate calmodulin. J. Biochem. 102: 1531-1537, 1987.
85. MADHAVAN, R., AND H. W. JARRETT. Calmodulin-activated phosphorylation of dystrophin. Biochemistry 33: 5797-5804, 1994.
86. MADHAVAN, R., AND H. W. JARRETT. Interactions between dystrophin glycoprotein complex proteins. Biochemistry 34: 12204-12209, 1995.
87. MADHAVAN, R., L. R. MASSOM, AND H. W. JARRETT. Calmodulin specifically binds three proteins of the dystrophin-glycoprotein complex. Biochem. Biophys. Res. Commun. 185: 753-759, 1992.
88. 2+ with the calmodulin-sensitive adenylate cyclase from Bordetella pertussis. J. Biol. Chem. 263: 6933-6940, 1988.
89. MEADOR, W. E., A. R. MEANS, AND F. QUIOCHO. Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures. Science 262: 1718-1721, 1993.
90. MEADOR, W. E., A. R. MEANS, AND F. QUIOCHO. Target enzyme recognition by calmodulin: 2,4 Å structure of a calmodulin-peptide complex. Science 257: 1261-1255, 1992.
91. MEANS, A. R., AND R. M. CONN (Editors). Cellular regulators. Calcium- and calmodulin-binding proteins. In: Methods in Enzymology. New York: Academic, 1987, vol. 139. pt. A, p. 3-846.
92. MEANS, A. R., J. S. TASH, AND J. G. CHAFOULEAS. Physiological implications of the presence, distribution, and regulation of calmodulin in eukaryotic cells. Physiol. Rev. 62: 1-39, 1982.
93. MEANS, A. R., M. F. A. VANBERKUM, I. BAGCHI, K. P. LU, AND C. D. RASMUSSEN. Regulatory function of calmodulin. Pharmacol. Ther. 50: 255-270, 1991.
94. 2+ and calmodulin. J. Bacteriol. 171: 1417-1422, 1989.
95. MOSER, M. J., M. R. FLORY, AND T. N. DAVIS. Calmodulin localizes to the spindly pole body of Schizosaccharomyces pombe and performs an essential function in chromosome segregation. J. Cell Sci. 110: 1805-1812, 1997.
96. 2+ binding to calmodulin and its role in Schizosaccharomyces pombe as revealed by mutagenesis and NMR spectroscopy. J. Biol. Chem. 270: 20643-20652, 1995.
97. 2+ regulates calmodulin binding to IQ motifs in IRS-1. Biochemistry 35: 15883-15889, 1996.
98. NEEL, V. A., AND M. W. YOUNG. Igloo, a GAP-43 related gene expressed in the developing nervous system of Drosophlia. Development 120: 2235-2243, 1994.
99. 2+-binding protein. Biochemistry 36: 1295-1305, 1997.
100. 2+-binding proteins. J. Biochem. 120: 685-698, 1996.
101. OHYA, Y., AND Y. ANRAKU. Functional expression of chicken calmodulin in yeast. Biochem. Biophys. Res. Commun. 158: 541-547, 1989.
102. OHYA, Y., AND Y. ANRAKU. A galactose-dependent cmd1 mutant of Saccharomyces cerevisiae: involvement of calmodulin in nuclear division. Curr. Genet. 15: 113-120, 1989.
103. OHYA, Y., AND D. BOTSTEIN. Diverse essential functions revealed by complementing yeast calmodulin mutants. Science 263: 963-966, 1994.
104. OHYA, Y., AND D. BOTSTEIN. Structure-based systematic isolation of conditional-lethal mutations in the single yeast calmodulin gene. Genetics 138: 1041-1054, 1994.
105. OHYA, Y., I. UNO, T. ISHIKAWA, AND Y. ANRAKU. Purification and biochemical properties of calmodulin from Saccharomyces cerevisiae. Eur. J. Biochem. 168: 13-19, 1987.
106. O'NEIL, K. T., AND W. F. DEGRADO. How calmodulin binds its targets: sequence independent recognition of amphiphilic alpha-helices. Trends Biochem. Sci. 15: 59-64, 1990.
107. 2+ mobilization. Proc. Natl. Acad. Sci. USA 94: 11627-11632, 1997.
108. 2+/calmodulin-dependent protein kinase genes in a unicellular eukaryote. EMBO J. 10: 1511-1522, 1991.
109. PERSECHINI, A., D. K. BLUMENTHAL, H. W. JARRETT, C. B. KLEE, D. O. HARDY, AND R. H. KRETSINGER. The effect of deletions in the central helix of calmodulin on enzyme activation and peptide binding. J. Biol. Chem. 264: 8052-8058, 1989.
110. PERSECHINI, A., AND R. H. KRETSINGER. The central helix of calmodulin functions as a flexible tether. J. Biol. Chem. 263: 12175-12178, 1988.
111. PERSECHINI, A., AND R. H. KRETSINGER. Toward a model of the calmodulin-myosin light-chain kinase complex: implications for calmodulin function. J. Cardiovasc. Pharmacol. 12, Suppl. 5: S1-S12, 1988.
112. PERSECHINI, A., R. H. KRETSINGER, AND T. N. DAVIS. Calmodulins with deletions in the central helix functionally replace the native protein in yeast cells. Proc. Natl. Acad. Sci. USA 88: 449-452, 1991.
113. PICTON, C., C. B. KLEE, AND P. COHEN. Phosphorylase kinase from rabbit skeletal muscle: identification of the calmodulin-binding subunits. Eur. J. Biochem. 111: 553-561, 1980.
114. PURDUE, R. L, M. A. KAETZEL, S. H. HAHN, B. R. BRINKLEY, AND J. R. DEDMAN. The identification of calmodulin-binding sites on mitochondria in cultured 3T3 cells. Cell 23: 533-542, 1981.
115. RASMUSSEN, C. D., AND A. R. MEANS. Calmodulin is involved in regulation of cell proliferation. EMBO J. 6: 3961-3968, 1987.
116. RASMUSSEN, C. D., R. L. MEANS, K. P. LU, G. S. MAY, AND A. R. MEANS. Characterization and expression of the unique calmodulin gene of Aspergillus nidulans. J. Biol. Chem. 265: 13767-13775, 1990.
117. RATAN, R. R., AND M. L. SHELANSKI. Calcium and the regulation of mitotic events. Trends Biochem. Sci. 11: 456-459, 1986.
118. RHOADS, A. R., AND F. FRIEDBERG. Sequence motifs for calmodulin recognition. FASEB J. 11: 331-340, 1997.
119. ROGEL, A., J. E. SCHULZ, R. M. BROWNLIE, J. G. COOTE, R. PARTON, AND E. HANSKI. Bordetella pertussis adenylate cyclase: purification and characterization of the active form of the enzyme. EMBO J. 8: 2755-2760, 1989.
120. 2+. J. Biol. Chem. 271: 22679-22686, 1996.
121. SALOMON, Y., C. LONDOS, AND M. RODBELL. A highly sensitive adenylate cyclase assay. Anal. Biochem. 58: 541-548, 1974.
122. SINGER, A. L., R. R. SHERWIN, A. S. DUNN, AND M. M. APPLEMAN. Cyclic nucleotide phosphodiesterases in neoplastic and non-neoplastic human mammary tissues. Cancer Res. 36: 60-66, 1976.
123. SLEMMON, J. R., J. I. MORGAN, S. M. FULLERTON, W. DANHO, B. S. HILBUSH, AND T. M. WENGENACK. Camstatins are peptide antagonists of calmodulin based upon a conserved structural motif in PEP-19, Neurogranin, and Neuromodulin. J. Biol. Chem. 271: 15911-15917, 1996.
124. SOBUE, K., R. YAMAZAKI, S. YASUDA, AND S. KAKIUCHI. Identity of the particulate form of calmodulin with soluble calmodulin. FEBS Lett. 129: 215-219, 1981.
125. STAROVASNIK, M. A., T. N. DAVIS, AND R. E. KLEVIT. Similarities and differences between yeast and vertebrate calmodulin: an examination of the calcium-binding and structural properties of calmodulin from the yeast Saccharomyces cerevisiae. Biochemistry 32: 3261-3270, 1993.
126. STIRLING, D. A., K. A. WELCH, AND M. J. STARK. Interaction with calmodulin is required for the function of Spc110p, an essential component of the yeast spindle pole body. EMBO J. 13: 4329-4342, 1994.
127. o is a major growth cone protein subject to regulation by GAP-43. Nature 344: 836-841, 1990.
128. STULL, J. T., K. E. KAMM, AND D. A. TAYLOR. Calcium control of smooth muscle contractility. Am. J. Med. Sci. 296: 241-245, 1988.
129. SUN, G. H., A HIRATA, Y. OHYA, AND Y. ANRAKU. Mutations in yeast calmodulin cause defects in spindle pole body functions and nuclear integrity. J. Cell Biol. 119: 1625-1639, 1992.
130. 2+-stimulated binding of myosin I to phosphatidylserine concerted with calmodulin dissociation. J. Biol. Chem. 267: 3445-3454, 1992.
131. SWEET, S. C., C. M. ROGERS, AND M. J. WELSH. Calmodulin stabilization of kinetochore microtubule structure to the effect of nocodazole. J. Cell Biol. 107: 2243-2251, 1988.
132. TAKEDA, T., Y. IMAI, AND M. YAMAMOTO. Substitution at position 116 of Schizosaccharomyces pombe calmodulin decreases its stability under nitrogen starvation and results in a sporulation-deficient phenotype. Proc. Natl. Acad. Sci. USA 86: 9737-9741, 1989.
133. TAKEDA, T., AND M. YAMAMOTO. Analysis and in vivo disruption of the gene coding for calmodulin in Schizosaccharomyces pombe. Proc. Natl. Acad. Sci. USA 84: 3580-3584, 1987.
134. 2+-dependent and independent binding of the modulator protein to the particulate fraction from brain. J. Cyclic Nucleotide Res. 4: 219-231, 1978.
135. TINSLEY, J. M., D. J. BLAKE, M. PEARCE, A. E. KNIGHT, J. KENDRICK-JONES, AND K. E. DAVIES. Dystrophin and related proteins. Curr. Opin. Genet. Dev. 3: 484-490, 1993.
136. TREWHELLA, J., D. K. BLUMENTHAL, S. E. ROKOP, AND P. A. SEEGER. Small-angle scattering studies show distinct conformations of calmodulin in its complexes with two peptides based on the regulatory domain of the catalytic subunit of phosphorylase kinase. Biochemistry 29: 9316-9324, 1990.
137. 2+ release channel (ryanodine receptor). Biophys. J. 69: 106-119, 1995.
138. UENISHI, K., W. E. CRISS, AND S. KAKIUCHI. Calcium-activatable phosphodiesterase and calcium-dependent modulator protein in transplantable hepatoma tissue. J. Biochem. 87: 601-607, 1980.
139. VAN HOOFF, C. O. M., P. N. E. DE GRAAN, A. B. OESTREICHER, AND W. H. GISPEN. B-50 phosphorylation and phosphoinositide metabolism in nerve growth cone membranes. J. Neurosci. 8: 1789-1795, 1988.
140. VENEMA, R. C., H. S. SAYEGH, J. D. KENT, AND D. G. HARISON. Identification, characterization, and comparison of the calmodulin-binding domains of the endothelial and inducible nitric oxide synthases. J. Biol. Chem. 271: 6435-6440, 1996.
141. VOGEL, H. J. Calmodulin: a versatile calcium mediator protein. Biochem. Cell Biol. 72: 357-376, 1994.
142. WANG, K. C., B. MUTUS, R. K. SHARMA, H.-Y. P. LAM, AND J. H. WANG. On the mechanism of interaction between calmodulin and calmodulin-dependent proteins. Can. J. Biochem. Cell Biol. 61: 911-920, 1983.
143. WANGSGARD, W. P., G. E. MEIXELL, M. DASGUPTA, AND D. K. BLUMENTHAL. Activation and inhibition of phosphorylase kinase by monospecific antibodies raised against peptides from the regulatory domain of the γ-subunit. J. Biol. Chem. 271: 21126-21133, 1996.
144. 2+-dependent modulator protein (calmodulin) of bovine brain. J. Biol. Chem. 255: 962-975, 1980.
145. WATTERSON, D. M., L. J. VAN ELDIK, R. E. SMITH, AND T. C. VANAMAN. Calcium-dependent regulatory protein of cyclic nucleotide metabolism in normal and transformed chicken embryo fibroblasts. Proc. Natl. Acad. Sci. USA 73: 2711-2715, 1976.
146. WEISSBACH, L., J. SETTLEMAN, M. F. KALADY, A. J. SNIJDER, A. E. MURTHY, Y. YAN, AND A. BERNARDS. Identification of a human RasGAP-related protein containing calmodulin-binding motifs. J. Biol. Chem. 269: 20517-20521, 1994.
147. 2+-binding and structural dynamics in the function of calmodulin. Annu. Rev. Physiol. 56: 213-236, 1994.
148. WOLENSKI, J. S. Regulation of calmodulin-binding myosins. Trends Cell Biol. 5: 310-316, 1995.
149. WYMAN, J. Linked functions and reciprocal effects in hemoglobin: a second look. Adv. Protein Chem. 19: 223-286, 1964.
150. XIE, Q., H. J. CHO, J. CALAYCAY, R. A. MUMFORD, K. M. SWIDEREK, T. D. LEE, A. DING, T. TROSO, AND C. NATHAN. Cloning and characterization of inducible nitric oxide synthase from mouse macrophages. Science 256: 225-228, 1992.
151. XIE, X., D. H. HARRISON, I. SCHLICHTING, R. M. SWEET, V. N. KALABOKIS, A. G. SZENT-GYORGYI, AND C. COHEN. Structure of the regulatory domain of scallop myosin at 2.8 Å resolution. Nature 368: 306-312, 1994.
152. 2+-independent stimulation of cyclic GMP-dependent protein kinase by calmodulin. Biochem. Biophys. Res. Commun. 94: 727-733, 1980.
153. YANG, B., D. JUNG, J. A. RAFAEL, J. S. CHAMBERLAIN, AND K. P. CAMPBELL. Identification of alpha-syntrophin binding to syntrophin triplet, dystrophin, and utrophin. J. Biol. Chem. 270: 4975-4978, 1995.
154. YANG, H., M. M. REEDY, C. L. BURKE, AND G. M. STRASBURG. Calmodulin interaction with the skeletal muscle sarcoplasmic reticulum calcium channel protein. Biochemistry 33: 518-525, 1994.
155. ZHANG, M., T. TANAKA, AND M. IKURA. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nature Struct. Biol. 2: 758-767, 1995.
156. ZUBER, M. X., S. M. STRITTMATTER, AND M. C. FISHMAN. A membrane-targeting signal in the amino-terminus of the neuronal protein GAP43. Nature 341: 345-348, 1989.
157. ZVELEBIL, M. J., AND J. M. THORNTON. Peptide-protein interactions: an overview. Q. Rev. Biophys. 26: 333-363, 1993.