Mouse A6/twinfilin is an actin monomer-binding protein that localizes to the regions of rapid actin dynamics

Molecular and Cellular Biology

Volumn 20, Issue 5, 2000, Pages 1772-1783

  Vartiainen, Maria ^a   Ojala, Pauli J ^a   Auvinen, Petri ^a   Peränen, Johan ^a   Lappalainen, Pekka ^a  

^a UNIVERSITY OF HELSINKI   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; CELL CYCLE PROTEIN; G ACTIN; ISOPROTEIN; MESSENGER RNA; PROTEIN TYROSINE KINASE; RAC PROTEIN; TWINFILIN; UNCLASSIFIED DRUG;

ACTIN FILAMENT; AMINO ACID SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CELL INTERACTION; CELLULAR DISTRIBUTION; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME ACTIVITY; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; TISSUE DISTRIBUTION;

ACTINS; AMINO ACID SEQUENCE; ANIMALS; CYTOSKELETON; GENE EXPRESSION REGULATION; MICE; MICROFILAMENT PROTEINS; MOLECULAR SEQUENCE DATA; ORGAN SPECIFICITY; RECOMBINANT PROTEINS; RNA, MESSENGER; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 0033976663     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.5.1772-1783.2000     Document Type: Article

References (35)

1. Arber, S., F. A. Barbayannis, H. Hanser, C. Schneider, C. A. Stanyon, O. Bernard, and P. Caroni. 1998. Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase. Nature 393:805-809.
2. Ausubel, F. M., R. Bruni, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.). 1990. Current protocols in molecular biology. John Wiley & Sons, New York, N.Y.
3. Hamburg, J. R., H. E. Harris, and A. Weeds. 1980. Partial purification and characterization of an actin depolymerizing factor from brain. FEBS Lett. 121:178-182.
4. Beeler, J. F., W. J. LaRochelle, M. Chedid, S. R. Tronick, and S. A. Aaronson. 1994. Procaryotic expression cloning of a novel human lyrosine kinase. Mol. Cell. Biol. 14:982-988.
5. Beeler, J. F., B. K. R. Patel, M. Chedid, and W. J. LaRochelle. 1997. Cloning and characterization of the mouse homolog of the human A6 gene. Gene 193:31-37.
6. lck at Tyr-505 and down regulates its catalytic activity. EMBO J. 11:2919-2924.
7. Blum, M., H. Beier, and H. J. Gross. 1987. Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8:93-99.
8. Carlier, M.-F., V. Laurent, J. Santolini, R. Melki, D. Didry, G.-X. Xia, Y. Hong, N.-H. Chua, and D. Pantaloni. 1997. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J. Cell Biol. 136:1307-1323.
9. Carlier, M.-F., and D. Pantaloni. 1997. Control of actin dynamics in cell motility. J. Mol. Biol. 269:459-467.
10. Goode, B. L., D. G. Drubin, and P. Lappalainen. 1998. Regulation of the cortical actin cytoskeleton in budding yeast by twinfilin, a ubiquitous actin monomer-sequestering protein. J. Cell Biol. 142:723-733.
11. Juuti, J. T., D. H. Bamford, R. Tuma, and G. J. Thomas. 1998. Structure and NTPase activity of the RNA-translocating protein (P4) of bacteriophage φ4. J. Mol. Biol. 279:347-359.
12. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
13. Lappalainen, P., E. V. Fedorov, A. A. Fedorov, S. C. Almo, and D. G. Drubin. 1997. Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis. EMBO J. 16:5520-5530.
14. Lappalainen, P., and D. G. Drubin. 1997. Cofilin promotes rapid actin filament turnover in vivo. Nature 388:78-82.
15. Lappalainen, P., M. M. Kessels, M. J. T. V. Cope, and D. G. Drubin. 1998. The ADF homology (ADF-H) domain, a highly exploited actin-binding module. Mol. Biol. Cell 9:1951-1959.
16. Lila, T., and D. G. Drubin. 1997. Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, and adenyl cyclase-associated protein and the actin cytoskeleton. Mol. Biol. Cell 8:367-385.
17. Machesky, L. M., and R. H. Insall. 1998. Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 8:1347-1356.
18. Maciver, S. K., H. G. Zot, and T. D. Pollard. 1991. Characterization of actin filament severing by actophorin from Acanthamoeba castellanii. J. Cell Biol. 115:1611-1620.
19. Morgan, T. E., R. O. Lockerbie, L. S. Minamide, M. D. Browning, and J. R. Bamburg. 1993. Isolation and characterization of a regulated form of actin depolymerizing factor. J. Cell Biol. 122:623-633.
20. Mullins, R. D., J. A. Heuser, and T. D. Pollard. 1998. The interaction of Arp2/3 complex with actin: nucleation, high-affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. USA 95:6181-6186.
21. Nagaoka, R., H. Abe, and T. Obinata. 1996. Site-directed mutagenesis of the phosphorylation site of cotilin: its role in cofilin-actin interaction and cytoplasmic localization. Cell Motil. Cytoskel. 35:200-209.
22. Nobes, C. D., and A. Hall. 1995. Rho, Rac, and cdc42 GTPases regulate the assembly of multimolecular local complexes associated with actin stress fibers, lamellipodia and filopodia. Cell 81:53-62.
23. Ohta, Y., E. Nishida, H. Sakai, and E. Miyamotu. 1989. Dephosphorylation of cofilin accompanies heat shock-induced nuclear accumulation of cofilin. J. Biol. Chem. 264:16143-16148.
24. Peränen, J., M. Rikkonen, M. Hyvönen, and L. Kääriäinen. 1996. T7 vectors with a modified T7lac promoter for expression of proteins in Escherichia coli. Anal. Biochem. 236:371-373.
25. Puius, Y. A., N. M. Mahoney, and S. C. Almo. 1998. The modular structure of actin regulatory proteins. Curr. Opin. Cell Biol. 10:23-34.
26. Ridley, A. J., and A. Hall. 1992. The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70:389-399.
27. Ridley, A. J., H. F. Paterson, C. L. Johnson, D. Diekmann, and A. Hall. 1992. The small GTP-binding protein Rac regulates growth factor-induced membrane ruffling. Cell 70:401-410.
28. Rosenblatt, J., B. J. Agnew. H. Abe, J. R. Hamburg, and T. J. Mitchison. 1947. Xenopus actin depolymerizing factor/cofilin XAC is responsible for the turnover of actin filaments in Listeria monocytogenes tails. J. Cell Biol. 136: 1323-1332.
29. Safer, D. 1981. An electrophoretic procedure for detecting proteins that bind actin monomers. Anal. Biochem. 178:32-37.
30. Sheterline, P., J. Clayton, and J. Sparrow. 1995. Actin. Protein Profile 2:1-103.
31. Shirao, T. 1995. The roles of microfilament-associated proteins, drebrins, in brain morphogenesis. J. Biochem. 117:231-236.
32. Van Troys, M., J. Vandekerckhove, and C. Ampe. 1999. Structural modules in actin-binding proteins: towards a new classification. Biochim. Biophys. Acta 1448:323-348.
33. Weber, A., C. R. Pennise, B. B. Babcock, and V. M. Fowler. 1994. Tropomodulin caps the pointed ends of actin filaments. J. Cell Biol. 127:1627-1635.
34. Welch, M. D., A. Iwamatsu, and T. J. Mitchison. 1997. Actin polymerization is induced by Arp2/3 complex at the surface of Listeria monocytogenes. Nature 385:265-269.
35. Yang, N., O. Higuchi, K. Ohashi, K. Nagata, A. Wada, K. Kangawa, E. Nishida, and K. Mizuno. 1998. Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature 393:809-812.