Abstract
Following the discovery of calmodulin (Kakiuchi et al. 1969, 1970; Cheung 1970), it was proposed that the contractile device of smooth muscle and the cytoskeleton of nonmuscle tissues may be regulated by Ca2+/calmodulin. Recently, we have obtained considerable amounts of evidence to support the view that the regulatory actions of Ca2+/calmodulin are mediated by a number of specific calmodulin-binding proteins which also bind to F-actin filaments or to tubulin (Kakiuchi and Sobue 1983). Caldesmon (Sobue et al. 1981a, b) from smooth muscle and tau factor (Sobue et al. 1981c) from brain microtubules are calmodulin-binding proteins which also bind to F-actin or tubulin, respectively. The Ca2+-dependent binding of calmodulin to these proteins obviated the interaction between these proteins and F-actin or tubulin. Therefore, the binding of these proteins to calmodulin and cytoskeletal proteins alternates, depending on the concentration of Ca2+ (Fig. 1). As the binding of the calmodulin-binding proteins to the target cytoskeletal proteins modulates the function of the latter proteins, calmodulin regulates the function of cytoskeletal proteins via these calmodulin-binding proteins. We named this type of regulatory action of calmodulin flip-flop regulation (Kakiuchi and Sobue 1981, see also Kakiuchi and Sobue 1983). This article is a brief description of these calmodulin-binding proteins.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
Adelstein RS, Sellers JR, Conti MA, Pato MD, de Lanerolle P (1982) Regulation of smooth muscle contractile proteins by calmodulin and cyclic AMP. Fed Proc 41: 2873–2878
Baines AJ (1983) The spread of spectrin. Nature (Lond) 301: 377–378
Bennett V, Davis J, Fowler WE (1982) Brain spectrin, a membrane-associated protein related in structure and function to erythrocyte spectrin. Nature (Lond) 299: 126–131
Branton D, Cohen CM, Tyler J (1981) Interaction of cytoskeletal proteins on the human erythrocyte membrane. Cell 24: 24–32
Cavadore JC, Molla A, Harricane MC, Gabrion J, Benyamin Y, Demaille JG (1982) Subcellular localization of myosin light chain kinase in skeletal, cardiac and smooth muscles. Proc Natl Sci USA 79: 3475–3479
Cheung WY (1970) Cyclic 3’,5’-nucleotide phosphodiesterase: demonstration of an activator. Biochem Biophys Res Commun 38: 533–538
Cleveland DW, Hwo SY, Kirschner MW (1977) Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin. J Mol Biol 116: 207–225
Cohen CM (1983) The molecular organization of the red cell membrane skeleton. Semin Hematol 20: 141–158
Dabrowska R, Hinkins S, Walsh MP, Hartshorne DJ (1982) The binding of smooth muscle myosin light chain kinase to actin. Biochem Biophy Res Commun 107: 1524–1531
Davies PJA, Klee CB (1981) Calmodulin-binding proteins: a high molecular weight calmodulinbinding protein from bovine brain. Biochem Int 3: 203–212
Ebashi S, Nanomura Y, Nakamura S, Nakasone H, Kohama K (1982) Regulatory mechanism in smooth muscle: actin-linked regulation. Fed. Proc 41: 2863–2867
Glenney JR, Glenney P, Osborn M, Weber K (1982a) An F-actin and calmodulin-binding protein from isolated intestinal brush borders has a morphology related to spectrin. Cell 28: 843–854
Glenney JR, Glenney P, Weber K (1982b) Erythroid spectrin, brain fodrin and intestinal brush-border proteins (TW-260/240) are related molecules containing a common calmodulin-binding subunit bound to a variant cell type-specific subunit. Proc Natl Acad Sci USA 79: 4002–4005
Guerriero Jr V, Rowley DR, Means AR (1981) Production and characterization of an antibody to myosim light chain kinase and intracellular localization of the enzyme. Cell 27: 449–458
Gshimura K, Ban T, Matsuda H, Fujita H, Sobue K, Kakiuchi S (1984) Immunocytochemical demonstration of caldesmon (a calmodulin-binding F-actin-interacting protein) in smooth muscle fibers and absorptive epithelial cells of the rat small intestine. Cell and Tissue Res 235: 207–209
Kakiuchi S, Sobue K (1981) Ca2+ and calmodulin-dependent flip-flop mechanism in the micro-tubule assembly-disassembly. FEBS Lett 132: 141–143
Kkiuchi S, Sobue K (1983) Control of cytoskeleton by calmodulin and calmodulin-binding proteins. Trends Biochem Sci 8: 59–62
Kakiuchi S, Yamazaki R, Nakajima H (1969) Studies on brain cyclic 3’,5’-nucleotide phosphodiesterase: its purification and properties (in Japanese). Bull Jpn Neurochem Soc 8: 17–20
Kakiuchi S, Yamazaki R, Nakajima H (1970) Properties of a heat-stable phosphodiesterase activating factor isolated from brain extract: studies on cyclic 3’,5’-nucleotide phosphodiesterase. II. Proc Jpn Acad 46: 587–592
Kakiuchi S, Sobue K, Fujita M (1981) Purification of a 240,000 dalton calmodulin-binding protein from a microsomal fraction of brain. FEBS Lett 132: 144–148
Kakiuchi S, Sobue K, Kanda K et al. (1982a) Correlative biochemical and morphological studies of brain calspectin: a spectrin-like calmodulin-binding protein. Biomed Res 3: 400–410
Kakiuchi S, Yasuda S, Yamazaki R, Teshima Y, Kanda K, Kakiuchi R, Sobue K (1982b) Quantitative determinations of calmodulin in the supernatant and particulate fractions of mammalian tissues. J Biochem (Tokyo) 92: 1041–1048
Kakiuchi S, Sobue K, Morimoto K, Kanda K (1982c) A spectrin-like calmodulin-binding protein (calspectin) of brain. Biochem Int 5: 755–762
Kakiuchi R, Inui M, Morimoto K, Kanda K, Sobue K, Kakiuchi S (1983) Caldesmon, a calmodulinbinding, F actin-interacting protein, is present in aorta, uterus and platelets. FEBS Lett 154: 351–356
Kumagai H, Nishida E, Sakai H (1982) The interaction between calmodulin and microtubule proteins. (IV) Quantitative analysis of the binding between calmodulin and tubulin dimer. J Biochem (Tokyo) 91: 1329–1336
de Lanerolle P, Adelstein RS, Feramisco JR, Burridge K (1981) Characterization of antibodies to smooth muscle myosin kinase and their use in localizing myosin kinase in nonmuscle cells. Proc Natl Acad Sci USA 78: 4738–4742
Lazarides E, Nelson WJ (1982) Expression of spectrin in nonerythroid cells. Cell 31:505–508 Levine J, Willard M (1981) Fodrin: axonally transported polypeptides associated with the internal periphery of many cells. J Cell Biol 90: 631–643
Means AR, Dedman JR (1980) Calmodulin: an intracellular calcium receptor. Nature (Lond) 285: 73–77
Morimoto K, Kambayashi J, Kosaki G, Kanda K, Sobue K, Kakiuchi S (1982) Calmodulin is the sole Ca2+-sensitizing factor in platelet myosin B. Biomed Res 3: 83–90
Owada MK, Hakura A, Iida K, Yahara I, Sobue K, Kakiuchi S (to be published 1984 ) Occurrence of caldesmon (a calmodulin-binding protein) in cells: comparison of normal and transformed cells. Proc Natl Acad Sci USA
Palfray HC, Schiebler W, Greengard P (1982) A major calmodulin-binding protein common to various vertebrate tissues. Proc Natl Acad Sci USA 79: 3780–3784
Shimooka T, Watanabe Y (1981) Stimulation of actomyosin Mg2+-ATPase activity by a brain microtubule-associated protein fraction. High-molecular weight actin-binding protein is the simulating factor. J Biochem (Tokyo) 90: 1297–1307
Sobue K, Muramoto Y, Yamazaki R, Kakiuchi S (1979) Distribution in rat tissues of modulator-binding protein of particulate nature: studies with [3H]modulator protein. FEBS Lett 105: 105–109
Sobue K, Fujita M, Muramoto Y, Kakiuchi S (1980) Spectrin as a major modulator binding protein of erythrocyte cytoskeleton. Biochem Int 1: 561–566
Sobue K, Muramoto Y, Fujita M, Kakiuchi S (1981a) Calmodulin-binding protein from chicken gizzard that interacts with F-actin. Biochem Int 2: 469–476
Sobue K, Muramoto Y, Fujita M, Kakiuchi S (1981b) Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin. Proc Natl Acad Sci USA 78: 5652–5655
Sobue K, Fujita M, Muramoto U, Kakiuchi S (1981c) The calmodulin-binding protein in micro-tubules is TAU factor. FEBS Lett 132: 137–140
Sobue K, Muramoto Y, Fujita M, Kakiuchi S (1981d) Calmodulin-binding protein of erythrocyte cytoskeleton. Biochem Biophys Res Commun 100: 1063–1070
Sobue K, Morimoto K, Kanda K, Maruyama K, Kakiuchi S (1982a) Reconstitution of Ca2+-sensitive gelation of actin filaments with filamin, caldesmon and calmodulin. FEBS Lett 138: 289–292
Sobue K, Morimoto K, Kanda K, Fukunaga K, Miyamoto E, Kakiuchi S (1982b) Interaction of 135000-M, calmodulin-binding protein (myosin kinase) and F-actin: another Cat+- and calmodulin-dependent flip-flop switch. Biochem Int 5: 503–510
Sobue K, Kanda K, Yamagami K, Kakiuchi S (1982c) Ca2+- and calmodulin-dependent phosphorylation of calspectin (spectrin-like calmodulin-binding protein; fodrin) by protein kinase system in synaptosomal cytosol and membranes. Biomed Res 3: 561–570
Sobue K, Kanda K, Kakiuchi S (1982d) Solubilization and partial purification of protein kinase systems from brain membranes that phosphorylate calspectin, a spectrin-like calmodulinbinding protein (fodrin). FEBS Lett 150: 185–190
Sobue K, Kanda K, Adachi J, Kakiuchi S (1983) Calmodulin-binding protein that interact with actin filaments in a Ca2+-dependent flip-flop manner: survery in brain and secretory tissues. Proc Natl Acad Sci USA 80: 6868–6871
Steck TL (1974) The organization of proteins in the human red blood cell membrane. J Cell Biol 62: 1–19
Stull JT, Silver PJ, Miller JR, Blumenthal DK, Botterman BR, Klug GA (1983) Phosphorylation of myosin light chain in skeletal and smooth muscles. Fed Proc 42: 21–26
Teshima Y, Kakiuchi S (1978) Membrane-bound forms of Ca2+-dependent protein modulator: Ca2+-dependent and independent bindings of modulator protein to the particulate fraction from brain. J Cyclic Nucleotide Res 4: 219–231
Timasheff SN, Grisham LM (1980) In vitro assembly of cytoplasmic microtubules. Annu Rev Biochem 49: 565–591
Tsukita S, Tsukita S, Ishikawa H, Kurokawa M, Morimoto K, Sobue K, Kakiuchi S (1983) Binding sites of calmodulin and actin on the brain spectrin, calspectin. J Cell Biol 97: 574–578
Walsh MP, Bridenbaugh R, Glenn W, Kerrick L, Hartshorne DJ (1983) Gizzard Ca2+-independent myosin light chain kinase: evidence in favor of the phosphorylation theory. Fed Proc 42: 45–50
Weisenberg RC (1972) Microtubule formation in vitro in solutions containing low calcium concentrations. Science (Wash DC) 177: 1104–1105
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1985 Springer-Verlag, Berlin Heidelberg
About this chapter
Cite this chapter
Kakiuchi, S. (1985). Biochemistry of the Ca2+- and Calmodulin-Dependent Regulation of the Cytoskeleton. In: Marmé, D. (eds) Calcium and Cell Physiology. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-70070-5_11
Download citation
DOI: https://doi.org/10.1007/978-3-642-70070-5_11
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-70072-9
Online ISBN: 978-3-642-70070-5
eBook Packages: Springer Book Archive