Detection of a sequence involved in actin-binding and phosphoinositide-binding in the N-terminal side of cofilin

Molecular and Cellular Biochemistry

Volumn 190, Issue 1-2, 1999, Pages 133-141

  Kusano, Ken Ichi ^a   Abe, Hiroshi ^b   Obinata, Takashi ^a,b  

^a UNIVERSITY OF TOKYO   (Japan)

^b CHIBA UNIVERSITY   (Japan)

Author keywords

Actin; Actin binding protein; Cofilin; Inositol phosphate

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; COFILIN; COMPLEMENTARY DNA; PEPTIDE; PHOSPHATIDYLINOSITIDE;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CLONING VECTOR; CROSS LINKING; ESCHERICHIA COLI; GENE CONSTRUCT; GENE DELETION; GENE EXPRESSION; NONHUMAN; OPEN READING FRAME; PROTEIN BINDING; PROTEIN DOMAIN; SEQUENCE ANALYSIS;

EID: 0033010590     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1007/978-1-4615-5543-8_17     Document Type: Article

References (45)

1. Nishida E, Maekawa S, Sakai H: Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropornyosin. Biochemistry 23: 5307-5313, 1984
2. Bamburg JR, Harris HE, Weeds AC: Partial purification and characterization of an actin depolymerizing factor. FEBS Lett 121: 178-181, 1980
3. Abe H, Endo T, Yamamoto K, Obinata T: Sequence of cDNAs encoding actin depolymerizing factor and cofilin of embryonic chicken skeletal muscle: Two functionally distinct actin-regulatory proteins exhibit high structural homology. Biochemistry 29: 7420-7425, 1990
4. Adams ME, Minamide LS, Deuster GL, Bamburg JR: Nucleotide sequence and expression of a cDNA encoding chick brain actin depolymerizing factor. Biochemistry 29: 7413-7419, 1990
5. McKim KS, Matheson C, Marra MA, Wakarchuk MF, Baillie DL: The Caenorhabditis elegans unc-60 gene encodes proteins homologous to a family of actin-binding proteins Mol Gen Genet 242: 346-357, 1994
6. Hayden SM, Miller PS, Brauweiler A, Bamburg JR: Analysis of the interactions of actin depolymerizing factor with G- and F-actin. Biochemistry 32: 9994-10004, 1993
7. Takagi T, Konishi K, Mabuchi I: Amino acid sequence of starfish oocyte depactin. J Biol Chem 263: 3097-3102, 1988
8. Sun H-Q, Kwiatkowska K, Yin HL: Actin monomer binding proteins. Curr Opin Cell Biol 7: 102-110, 1995
9. Gunsalus KC, Bonaccorsi S, Williams E, Verni F, Gatti M, Goldberg ML: Mutation in twinster, a Drosophila gene encoding a cofilin/ADF homologue, results in defects in centrosome migration and cytokinesis. J Cell Biol 131: 1243-1259, 1995
10. Matsuzaki F, Matsumoto F, Yahara I, Yonezawa N, Nishida E, Sakai H: Cloning and characterization of porcine brain cofilin cDNA. J Biol Chem 263: 11564-11568, 1988
11. r actin binding and depolymerizing. Gene (Amst) 124: 115-120, 1993
12. Moon AL, Janmey P, Louie KA, Drubin D: Cofilin is an essential component of the yeast cortical cytoskeleton. J Cell Biol 120: 421-435, 1993
13. Abe H, Obinata T, Minamide LS, Bamburg JR: Xenopus laevis actin-depolymerizing factor/cofilin: A phosphorylation-regulated protein essential for development. J Cell Biol 132: 871-885, 1996
14. Nagaoka R, Abe H, Kusano K, Obinata T: Concentration of cofilin, a small actin-binding protein, at the cleavage furrow during cytokinesis. Cell Motil Cytoskeleton 30: 1-7, 1995
15. Abe H, Ohshima S, Obinata T: A cofilin-like protein is involved in the regulation of actin assembly in developing skeletal muscle. J Biochem (Tokyo) 106: 696-702, 1989
16. Obinata T: Contractile proteins and myofibrillogenesis. Int Rev Cytol 143: 153-189, 1993
17. Nagaoka R, Kusano K Abe H, Obinata T: Effects of cofilin on actin filamentous structures in cultured muscle cells: Intracellular regulation of cofilin action. J Cell Sci 108: 581-593, 1995
18. Yonezawa N, Nishida E, Sakai H: pH control of actin polymerization of cofilin. J Biol Chem 260: 14410-14412, 1985
19. Yonezawa N, Nishida E, Iida K, Yahara I, Sakai H: Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides. J Biol Chem 265: 8382-8386, 1990
20. Moriyama K, Iida K, Yahara I: Phosphorylation of Ser-3 of cofilin regulates its essential function on actin. Genes to Cells 1: 73-86, 1996
21. Agnew BJ, Minamide LS, Bamburg JR: Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J Biol Chem 270: 17582-17587, 1995
22. Yonezawa N, Nishida E, Iida K, Kumagai H, Yahara I, Sakai H: Inhibition of actin polymerization by a synthetic dodecapeptide patterned on the sequence around the actin-binding site of cofilin. J Biol Chem 266: 10485-10489, 1991
23. Yonezawa N, Homma Y, Yahara I, Sakai H, Nishida E: A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin. J Biol Chem 266: 17218-17221, 1991
24. Abe H, Nagaoka R, Obinata T: Cytoplasmic localization and nuclear transport of cofilin in cultured myotubes. Exp Cell Res 206: 1-10, 1993
25. Iida K, Matsumoto S, Yahara I: The KKRKK sequence is involved in heat shock-induced nuclear translocation of the 18-kDa actin-binding protein, cofilin. Cell Struct Funct 17: 39-46, 1992
26. Spudich JA, Watt S: The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the tropomyosin-troponin complex with actin and the proteolytic fragment of myosin. J Biol Chem 246: 4866-4871, 1971
27. Higashi S, Oosawa F: Conformational changes associated with polymerization and nucleotide binding in actin binding. J Mol Biol 112: 843-865, 1965
28. Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970
29. Itzaki RF, Gill DM: A micro-biuret method for estimating proteins. Analyt Biochem 9: 401-410, 1964
30. Janmey PA, Lamb J, Allen PC, Matsudaira PT: Phosphoinisitide-binding peptides derived from the sequences of gelsolin and villin. J Biol Chem 267: 11818-11823, 1992
31. Yonezawa N, Nishida E, Ohba M, Seki M, Kumagai H, Sakai H: An actin-interacting peptide in the cofilin sequence. Eur J Biochem 183 235-238, 1989
32. Moriyama K Yonezawa N, Sakai H, Yahara I, Nishida E: Mutational analysis of an actin-binding site of cofilin and characterization of chimeric proteins between cofilin and destrin. J Biol Chem 267: 7240-7244, 1992
33. Yu F-X, Sun HQ, Janmey PA, Yin HL: Identification of a polyphosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin. J Biol Chem 267: 14616-14621, 1992
34. Matsudaira P, Janmey P: Pieces in the actin-severing protein puzzle. Cell 54: 139-140, 1988
35. Hatanaka H, Ogura K, Moriyama K, Ichikawa S, Yahara I, Inagaki F: Tertiary structure of destrin and structural similarity between two actin-regulating protein families. Cell 85: 1047-1055, 1996
36. Rudin CM, Englaer P, Storb U: Differential splicing of thymosin β4 mRNA. J Immunol 144: 4857-4862, 1990
37. Erickson-Viitanen S, Ruggieri S, Natalini P, Horcker BL: Distribution of thymosin β4 in vertebrate classes. Arch Biochem Biophys 221: 570-576, 1983
38. Ono S, Minami N, Abe H, ObinataT: Characterization of a novel cofilin isoform that is predominantly expressed in mammalian skeletal muscle. J Biol Chem 269: 15280-15286, 1994
39. Moriyama K, Matsumoto S, Nishida E, Sakai H, Yahara I: Nucleotide sequence of mouse cofilin cDNA. Nucl Acids Res 18: 3053, 1990
40. Moriyama K, Nishida E, Yonezawa N, Sakai H, Matsumoto S, Iida K, I: Destrin, a mammalian actin-depolymerizing protein, is closely related to cofilin. Cloning and expression of porcine brain destrin cDNA. J Biol Chem 265: 5771-5773, 1990
41. Quirk S, Maciver SK, Ampe C, Doberstin SK, Kaise DA, VanDamme J, Vadekerckhove JS, Pollard TD: Primary structure of and studies on Acanthamoeba actophorin. Biochemistry 32: 8525-8533, 1993
42. Kim S-R, Kim Y, An G: Molecular cloning and characterization of antherpreferential cDNA encoding a putative actin-depolymerizing factor. Plat Mol Biol 21: 39-45, 1993
43. Kwiatowski DJ, Stossel TP, Orkin SH, Mole JE, Colten HR, Yin HL: Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain. Nature 323: 455-488, 1986
44. Dabiri GA, Young CL, Rosenbloom J, Southwick FS: Molecular cloning of human macrophage capping protein cDNA. A unique member of the gelsolin/villin family expressed primarily in macrophage. J Biol Chem 267: 16545-16552, 1992
45. Bazari WL, Matsudaira P, Wallek M, Smeal. T, Jakes R, Asmed Y: Villin sequence and peptide map identify six homologous domains. Proc Natl Acad Sci USA 85: 4986-4990, 1988