메뉴 건너뛰기




Volumn 288, Issue 4, 2013, Pages 2464-2474

Phosphorylation of actin-related protein 2 (Arp2) is required for normal development and cAMP chemotaxis in dictyostelium

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN-RELATED PROTEINS; ARP2/3 COMPLEX; DICTYOSTELIUM; DROSOPHILA CELLS; F-ACTIN; MUTANT CELLS; NUCLEATING ACTIVITY; TYROSINE RESIDUES; VEGETATIVE CELLS; WILD-TYPE CELLS;

EID: 84873800955     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.435313     Document Type: Article
Times cited : (15)

References (41)
  • 1
    • 70249116807 scopus 로고    scopus 로고
    • Actin dynamics at the leading edge: From simple machinery to complex networks
    • Insall, R. H., and Machesky, L. M. (2009) Actin dynamics at the leading edge: from simple machinery to complex networks. Dev. Cell 17, 310-322
    • (2009) Dev. Cell , vol.17 , pp. 310-322
    • Insall, R.H.1    MacHesky, L.M.2
  • 2
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: Nucleation, high affinity pointed end capping, and formation of branching networks of filaments
    • Mullins, R. D., Heuser, J. A., and Pollard, T. D. (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. U.S.A. 95, 6181-6186
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 3
    • 0035094485 scopus 로고    scopus 로고
    • The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments
    • Amann, K. J., and Pollard, T. D. (2001) The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments. Nat. Cell Biol. 3, 306-310
    • (2001) Nat. Cell Biol. , vol.3 , pp. 306-310
    • Amann, K.J.1    Pollard, T.D.2
  • 4
    • 33749037156 scopus 로고    scopus 로고
    • The ARP2/3 complex: An actin nucleator comes of age
    • Goley, E. D., and Welch, M. D. (2006) The ARP2/3 complex: an actin nucleator comes of age. Nat. Rev. Mol. Cell Biol. 7, 713-726
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 713-726
    • Goley, E.D.1    Welch, M.D.2
  • 5
    • 0033576288 scopus 로고    scopus 로고
    • Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization
    • Higgs, H. N., Blanchoin, L., and Pollard, T. D. (1999) Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization. Biochemistry 38, 15212-15222
    • (1999) Biochemistry , vol.38 , pp. 15212-15222
    • Higgs, H.N.1    Blanchoin, L.2    Pollard, T.D.3
  • 8
  • 9
    • 81355154116 scopus 로고    scopus 로고
    • Phosphorylation of the Arp2 subunit relieves auto-inhibitory interactions for Arp2/3 complex activation
    • Narayanan, A., LeClaire, L. L., 3rd, Barber, D. L., and Jacobson, M. P. (2011) Phosphorylation of the Arp2 subunit relieves auto-inhibitory interactions for Arp2/3 complex activation. PLoS Comput. Biol. 7, e1002226
    • (2011) PLoS Comput. Biol. , vol.7
    • Narayanan, A.1    Leclaire Iii, L.L.2    Barber, D.L.3    Jacobson, M.P.4
  • 11
    • 34447282292 scopus 로고    scopus 로고
    • Replacement of the essential Dictyostelium Arp2 gene by its Entamoeba homologue using parasexual genetics
    • Zaki, M., King, J., Fütterer, K., and Insall, R. H. (2007) Replacement of the essential Dictyostelium Arp2 gene by its Entamoeba homologue using parasexual genetics. BMC Genet. 8, 28
    • (2007) BMC Genet , vol.8 , pp. 28
    • Zaki, M.1    King, J.2    Fütterer, K.3    Insall, R.H.4
  • 12
    • 34250832113 scopus 로고    scopus 로고
    • Mutants in the Dictyostelium Arp2/3 complex and chemoattractant-induced actin polymerization
    • Langridge, P. D., and Kay, R. R. (2007) Mutants in the Dictyostelium Arp2/3 complex and chemoattractant-induced actin polymerization. Exp. Cell Res. 313, 2563-2574
    • (2007) Exp. Cell Res. , vol.313 , pp. 2563-2574
    • Langridge, P.D.1    Kay, R.R.2
  • 13
    • 77956695449 scopus 로고    scopus 로고
    • Expression of actin-interacting protein 1 suppresses impaired chemotaxis of Dictyostelium cells lacking the Na -H exchanger NHE1
    • Choi, C.-H., Patel, H., and Barber, D. L. (2010) Expression of actin-interacting protein 1 suppresses impaired chemotaxis of Dictyostelium cells lacking the Na -H exchanger NHE1. Mol. Biol. Cell 21, 3162-3170
    • (2010) Mol. Biol. Cell , vol.21 , pp. 3162-3170
    • Choi, C.-H.1    Patel, H.2    Barber, D.L.3
  • 15
    • 58849149327 scopus 로고    scopus 로고
    • Anew set of small, extrachromosomal expression vectors for Dictyostelium discoideum
    • Veltman, D. M., Akar, G., Bosgraaf, L., and Van Haastert, P. J. (2009)Anew set of small, extrachromosomal expression vectors for Dictyostelium discoideum. Plasmid 61, 110-118
    • (2009) Plasmid , vol.61 , pp. 110-118
    • Veltman, D.M.1    Akar, G.2    Bosgraaf, L.3    Van Haastert, P.J.4
  • 16
    • 79955545833 scopus 로고    scopus 로고
    • Functional analysis of Dictyostelium IBARa reveals a conserved role of the I-BAR domain in endocytosis
    • Veltman, D. M., Auciello, G., Spence, H. J., Machesky, L. M., Rappoport, J. Z., and Insall, R. H. (2011) Functional analysis of Dictyostelium IBARa reveals a conserved role of the I-BAR domain in endocytosis. Biochem. J. 436, 45-52
    • (2011) Biochem. J. , vol.436 , pp. 45-52
    • Veltman, D.M.1    Auciello, G.2    Spence, H.J.3    MacHesky, L.M.4    Rappoport, J.Z.5    Insall, R.H.6
  • 17
    • 34547738614 scopus 로고    scopus 로고
    • Possible roles of the endocytic cycle in cell motility
    • Traynor, D., and Kay, R. R. (2007) Possible roles of the endocytic cycle in cell motility. J. Cell Sci. 120, 2318-2327
    • (2007) J. Cell Sci. , vol.120 , pp. 2318-2327
    • Traynor, D.1    Kay, R.R.2
  • 18
    • 84859613693 scopus 로고    scopus 로고
    • Pseudopod growth and evolution during cell movement is controlled through SCAR/WAVE dephosphorylation
    • Ura, S., Pollitt, A. Y., Veltman, D. M., Morrice, N. A., Machesky, L. M., and Insall, R. H. (2012) Pseudopod growth and evolution during cell movement is controlled through SCAR/WAVE dephosphorylation. Curr. Biol. 22, 553-561
    • (2012) Curr. Biol. , vol.22 , pp. 553-561
    • Ura, S.1    Pollitt, A.Y.2    Veltman, D.M.3    Morrice, N.A.4    MacHesky, L.M.5    Insall, R.H.6
  • 19
    • 77952955309 scopus 로고    scopus 로고
    • Understanding eukaryotic chemotaxis: A pseudopodcentered view
    • Insall, R. H. (2010) Understanding eukaryotic chemotaxis: a pseudopodcentered view. Nat. Rev. Mol. Cell Biol. 11, 453-458
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 453-458
    • Insall, R.H.1
  • 20
    • 0042921214 scopus 로고    scopus 로고
    • PIR121 regulates pseudopod dynamics and SCAR activity in Dictyostelium
    • Blagg, S. L., Stewart, M., Sambles, C., and Insall, R. H. (2003) PIR121 regulates pseudopod dynamics and SCAR activity in Dictyostelium. Curr. Biol. 13, 1480-1487
    • (2003) Curr. Biol. , vol.13 , pp. 1480-1487
    • Blagg, S.L.1    Stewart, M.2    Sambles, C.3    Insall, R.H.4
  • 21
    • 0032734244 scopus 로고    scopus 로고
    • Circulation of the plasma membrane in Dictyostelium
    • Aguado-Velasco, C., and Bretscher, M. S. (1999) Circulation of the plasma membrane in Dictyostelium. Mol. Biol. Cell 10, 4419-4427
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4419-4427
    • Aguado-Velasco, C.1    Bretscher, M.S.2
  • 22
    • 1642446043 scopus 로고    scopus 로고
    • P41-Arc subunit of human Arp2/3 complex is a p21-activated kinase- 1-interacting substrate
    • Vadlamudi, R. K., Li, F., Barnes, C. J., Bagheri-Yarmand, R., and Kumar, R. (2004) p41-Arc subunit of human Arp2/3 complex is a p21-activated kinase- 1-interacting substrate. EMBO Rep. 5, 154-160
    • (2004) EMBO Rep. , vol.5 , pp. 154-160
    • Vadlamudi, R.K.1    Li, F.2    Barnes, C.J.3    Bagheri-Yarmand, R.4    Kumar, R.5
  • 23
    • 0141480959 scopus 로고    scopus 로고
    • Identification of the p16-Arc subunit of the Arp 2/3 complex as a substrate of MAPK-activated protein kinase 2 by proteomic analysis
    • Singh, S., Powell, D. W., Rane, M. J., Millard, T. H., Trent, J. O., Pierce, W. M., Klein, J. B., Machesky, L. M., and McLeish, K. R. (2003) Identification of the p16-Arc subunit of the Arp 2/3 complex as a substrate of MAPK-activated protein kinase 2 by proteomic analysis. J. Biol. Chem. 278, 36410-36417
    • (2003) J. Biol. Chem. , vol.278 , pp. 36410-36417
    • Singh, S.1    Powell, D.W.2    Rane, M.J.3    Millard, T.H.4    Trent, J.O.5    Pierce, W.M.6    Klein, J.B.7    MacHesky, L.M.8    McLeish, K.R.9
  • 26
    • 77949834455 scopus 로고    scopus 로고
    • A nucleator arms race cellular control of actin assembly
    • Campellone, K. G., and Welch, M. D. (2010) A nucleator arms race: cellular control of actin assembly. Nat. Rev. Mol. Cell Biol. 11, 237-251
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 237-251
    • Campellone, K.G.1    Welch, M.D.2
  • 27
    • 0037442388 scopus 로고    scopus 로고
    • ForC, a novel type of formin family protein lacking an FH1 domain, is involved in multicellular development in Dictyostelium discoideum
    • Kitayama, C., and Uyeda, T. Q. (2003) ForC, a novel type of formin family protein lacking an FH1 domain, is involved in multicellular development in Dictyostelium discoideum. J. Cell Sci. 116, 711-723
    • (2003) J. Cell Sci. , vol.116 , pp. 711-723
    • Kitayama, C.1    Uyeda, T.Q.2
  • 28
    • 20444426470 scopus 로고    scopus 로고
    • The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia
    • Schirenbeck, A., Bretschneider, T., Arasada, R., Schleicher, M., and Faix, J. (2005) The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia. Nat. Cell Biol. 7, 619-625
    • (2005) Nat. Cell Biol. , vol.7 , pp. 619-625
    • Schirenbeck, A.1    Bretschneider, T.2    Arasada, R.3    Schleicher, M.4    Faix, J.5
  • 29
    • 77956239261 scopus 로고    scopus 로고
    • Expression of Y53A-actin in Dictyostelium disrupts the cytoskeleton and inhibits intracellular and intercellular chemotactic signaling
    • Shu, S., Liu, X., Kriebel, P. W., Hong, M. S., Daniels, M. P., Parent, C. A., and Korn, E. D. (2010) Expression of Y53A-actin in Dictyostelium disrupts the cytoskeleton and inhibits intracellular and intercellular chemotactic signaling. J. Biol. Chem. 285, 27713-27725
    • (2010) J Biol Chem , vol.285 , pp. 27713-27725
    • Shu, S.1    Liu, X.2    Kriebel, P.W.3    Hong, M.S.4    Daniels, M.P.5    Parent, C.A.6    Korn, E.D.7
  • 30
    • 84862907778 scopus 로고    scopus 로고
    • Actin cross-linking proteins cortexillin i and II are required for cAMP signaling during Dictyostelium chemotaxis and development
    • Shu, S., Liu, X., Kriebel, P. W., Daniels, M. P., and Korn, E. D. (2012) Actin cross-linking proteins cortexillin I and II are required for cAMP signaling during Dictyostelium chemotaxis and development. Mol. Biol. Cell 23, 390-400
    • (2012) Mol. Biol. Cell , vol.23 , pp. 390-400
    • Shu, S.1    Liu, X.2    Kriebel, P.W.3    Daniels, M.P.4    Korn, E.D.5
  • 31
    • 67650081142 scopus 로고    scopus 로고
    • The Arp2/3 complex andWASpare required for apical trafficking of Delta into microvilli during cell fate specification of sensory organ precursors
    • Rajan, A., Tien, A. C., Haueter, C. M., Schulze, K. L., and Bellen, H. J. (2009) The Arp2/3 complex andWASpare required for apical trafficking of Delta into microvilli during cell fate specification of sensory organ precursors. Nat. Cell Biol. 11, 815-824
    • (2009) Nat. Cell Biol. , vol.11 , pp. 815-824
    • Rajan, A.1    Tien, A.C.2    Haueter, C.M.3    Schulze, K.L.4    Bellen, H.J.5
  • 33
    • 0344796392 scopus 로고    scopus 로고
    • Two phases of actin polymerization display different dependencies on PI(34 5P3 accumulation and have unique roles during chemotaxis
    • Chen, L., Janetopoulos, C., Huang, Y. E., Iijima, M., Borleis, J., and Devreotes, P. N. (2003) Two phases of actin polymerization display different dependencies on PI(3,4,5)P3 accumulation and have unique roles during chemotaxis. Mol. Biol. Cell 14, 5028-5037
    • (2003) Mol Biol Cell , vol.14 , pp. 5028-5037
    • Chen, L.1    Janetopoulos, C.2    Huang, Y.E.3    Iijima, M.4    Borleis, J.5    Devreotes, P.N.6
  • 34
    • 80055075385 scopus 로고    scopus 로고
    • Direct biochemical measurements of signal relay during Dictyostelium development
    • Das, S., Rericha, E. C., Bagorda, A., and Parent, C. A. (2011) Direct biochemical measurements of signal relay during Dictyostelium development. J. Biol. Chem. 286, 38649-38658
    • (2011) J. Biol. Chem. , vol.286 , pp. 38649-38658
    • Das, S.1    Rericha, E.C.2    Bagorda, A.3    Parent, C.A.4
  • 35
    • 34247372469 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 3-kinases in chemotaxis in Dictyostelium
    • Takeda, K., Sasaki, A. T., Ha, H., Seung, H. A., and Firtel, R. A. (2007) Role of phosphatidylinositol 3-kinases in chemotaxis in Dictyostelium. J. Biol. Chem. 282, 11874-11884
    • (2007) J. Biol. Chem. , vol.282 , pp. 11874-11884
    • Takeda, K.1    Sasaki, A.T.2    Ha, H.3    Seung, H.A.4    Firtel, R.A.5
  • 36
    • 0034721696 scopus 로고    scopus 로고
    • Integration of multiple signals through cooperative regulation of the N-WASPArp2/3 complex
    • Prehoda, K. E., Scott, J. A., Mullins, R. D., and Lim, W. A. (2000) Integration of multiple signals through cooperative regulation of the N-WASPArp2/3 complex. Science 290, 801-806
    • (2000) Science , vol.290 , pp. 801-806
    • Prehoda, K.E.1    Scott, J.A.2    Mullins, R.D.3    Lim, W.A.4
  • 37
    • 0034683746 scopus 로고    scopus 로고
    • Mechanism of NWASP activation by CDC42 and phosphatidylinositol 4,5-bisphosphate
    • Rohatgi, R., Ho, H. Y., and Kirschner, M. W. (2000) Mechanism of NWASP activation by CDC42 and phosphatidylinositol 4,5-bisphosphate. J. Cell Biol. 150, 1299-1310
    • (2000) J. Cell Biol. , vol.150 , pp. 1299-1310
    • Rohatgi, R.1    Ho, H.Y.2    Kirschner, M.W.3
  • 38
    • 0034683671 scopus 로고    scopus 로고
    • Activation by Cdc42 and PIP2 of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex
    • Higgs, H. N., and Pollard, T. D. (2000) Activation by Cdc42 and PIP2 of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex. J. Cell Biol. 150, 1311-1320
    • (2000) J. Cell Biol. , vol.150 , pp. 1311-1320
    • Higgs, H.N.1    Pollard, T.D.2
  • 40
    • 84863229890 scopus 로고    scopus 로고
    • Arp2/3 is critical for lamellipodia and response to extracellular matrix cues but is dispensable for chemotaxis
    • Wu, C., Asokan, S. B., Berginski, M. E., Haynes, E. M., Sharpless, N. E., Griffith, J. D., Gomez, S. M., and Bear, J. E. (2012) Arp2/3 is critical for lamellipodia and response to extracellular matrix cues but is dispensable for chemotaxis. Cell 148, 973-987
    • (2012) Cell , vol.148 , pp. 973-987
    • Wu, C.1    Asokan, S.B.2    Berginski, M.E.3    Haynes, E.M.4    Sharpless, N.E.5    Griffith, J.D.6    Gomez, S.M.7    Bear, J.E.8
  • 41
    • 84861926483 scopus 로고    scopus 로고
    • The Arp2/3 complex is required for lamellipodia extension and directional fibroblast cell migration
    • Suraneni, P., Rubinstein, B., Unruh, J. R., Durnin, M., Hanein, D., and Li, R. (2012) The Arp2/3 complex is required for lamellipodia extension and directional fibroblast cell migration. J. Cell Biol. 197, 239-251
    • (2012) J. Cell Biol. , vol.197 , pp. 239-251
    • Suraneni, P.1    Rubinstein, B.2    Unruh, J.R.3    Durnin, M.4    Hanein, D.5    Li, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.