메뉴 건너뛰기




Volumn 125, Issue 23, 2012, Pages 5860-5872

G-actin regulates the shuttling and PP1 binding of the RPEL protein Phactr1 to control actomyosin assembly

Author keywords

Actin; Actomyosin; Phactr; PP1; RPEL

Indexed keywords

CELL PROTEIN; G ACTIN; KARYOPHERIN ALPHA; KARYOPHERIN BETA; MYOSIN ADENOSINE TRIPHOSPHATASE; PHOSPHATASE AND ACTIN REGULATOR PROTEIN 1; PP1 PROTEIN; UNCLASSIFIED DRUG;

EID: 84868584901     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.112078     Document Type: Article
Times cited : (51)

References (48)
  • 3
    • 77955279255 scopus 로고    scopus 로고
    • The extended PP1 toolkit: designed to create specificity
    • Bollen, M., Peti, W., Ragusa, M. J. and Beullens, M. (2010). The extended PP1 toolkit: designed to create specificity. Trends Biochem. Sci. 35, 450-458.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 450-458
    • Bollen, M.1    Peti, W.2    Ragusa, M.J.3    Beullens, M.4
  • 4
    • 0346728803 scopus 로고    scopus 로고
    • Functional diversity of protein phosphatase-1, a cellular economizer and reset button
    • Ceulemans, H. and Bollen, M. (2004). Functional diversity of protein phosphatase-1, a cellular economizer and reset button. Physiol. Rev. 84, 1-39.
    • (2004) Physiol. Rev. , vol.84 , pp. 1-39
    • Ceulemans, H.1    Bollen, M.2
  • 6
    • 79957608812 scopus 로고    scopus 로고
    • Scapinin-induced inhibition of axon elongation is attenuated by phosphorylation and translocation to the cytoplasm
    • Farghaian, H., Chen, Y., Fu, A. W., Fu, A. K., Ip, J. P., Ip, N. Y., Turnley, A. M. and Cole, A. R. (2011). Scapinin-induced inhibition of axon elongation is attenuated by phosphorylation and translocation to the cytoplasm. J. Biol. Chem. 286, 19724-19734.
    • (2011) J. Biol. Chem. , vol.286 , pp. 19724-19734
    • Farghaian, H.1    Chen, Y.2    Fu, A.W.3    Fu, A.K.4    Ip, J.P.5    Ip, N.Y.6    Turnley, A.M.7    Cole, A.R.8
  • 7
    • 11144322399 scopus 로고    scopus 로고
    • Overexpression of a family of RPEL proteins modifies cell shape
    • Favot, L., Gillingwater, M., Scott, C. and Kemp, P. R. (2005). Overexpression of a family of RPEL proteins modifies cell shape. FEBS Lett. 579, 100-104.
    • (2005) FEBS Lett , vol.579 , pp. 100-104
    • Favot, L.1    Gillingwater, M.2    Scott, C.3    Kemp, P.R.4
  • 8
    • 0041574981 scopus 로고
    • Studies on the composition and polymerization of actin
    • Feuer, G., Molnar, F., Pettko, E. and Straub, F. B. (1948). Studies on the composition and polymerization of actin. Hung. Acta Physiol. 1, 150-163.
    • (1948) Hung. Acta Physiol. , vol.1 , pp. 150-163
    • Feuer, G.1    Molnar, F.2    Pettko, E.3    Straub, F.B.4
  • 9
    • 65249111020 scopus 로고    scopus 로고
    • Actin dynamics and functions in the interphase nucleus: moving toward an understanding of nuclear polymeric actin
    • Gieni, R. S. and Hendzel, M. J. (2009). Actin dynamics and functions in the interphase nucleus: moving toward an understanding of nuclear polymeric actin. Biochem. Cell Biol. 87, 283-306.
    • (2009) Biochem. Cell Biol. , vol.87 , pp. 283-306
    • Gieni, R.S.1    Hendzel, M.J.2
  • 10
    • 37849015440 scopus 로고    scopus 로고
    • RPEL motifs link the serum response factor cofactor MAL but not myocardin to Rho signaling via actin binding
    • Guettler, S., Vartiainen, M. K., Miralles, F., Larijani, B. and Treisman, R. (2008). RPEL motifs link the serum response factor cofactor MAL but not myocardin to Rho signaling via actin binding. Mol. Cell. Biol. 28, 732-742.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 732-742
    • Guettler, S.1    Vartiainen, M.K.2    Miralles, F.3    Larijani, B.4    Treisman, R.5
  • 11
    • 0025261344 scopus 로고
    • Application of fluorescence energy transfer and polarization to monitor Escherichia coli cAMP receptor protein and lac promoter interaction
    • Heyduk, T. and Lee, J. C. (1990). Application of fluorescence energy transfer and polarization to monitor Escherichia coli cAMP receptor protein and lac promoter interaction. Proc. Natl. Acad. Sci. USA 87, 1744-1748.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1744-1748
    • Heyduk, T.1    Lee, J.C.2
  • 12
    • 80054842900 scopus 로고    scopus 로고
    • Sensing actin dynamics: structural basis for G-actin-sensitive nuclear import of MAL
    • Hirano, H. and Matsuura, Y. (2011). Sensing actin dynamics: structural basis for G-actin-sensitive nuclear import of MAL. Biochem. Biophys. Res. Commun. 414, 373-378.
    • (2011) Biochem. Biophys. Res. Commun. , vol.414 , pp. 373-378
    • Hirano, H.1    Matsuura, Y.2
  • 14
    • 70749096913 scopus 로고    scopus 로고
    • Genome-wide association of early-onset myocardial infarction with single nucleotide polymorphisms and copy number variants
    • Myocardial Infarction Genetics Consortium; Wellcome Trust Case Control Consortium
    • Kathiresan, S., Voight, B. F., Purcell, S., Musunuru, K., Ardissino, D., Mannucci, P. M., Anand, S., Engert, J. C., Samani, N. J., Schunkert, H. et al.; Myocardial Infarction Genetics Consortium; Wellcome Trust Case Control Consortium (2009). Genome-wide association of early-onset myocardial infarction with single nucleotide polymorphisms and copy number variants. Nat. Genet. 41, 334-341.
    • (2009) Nat. Genet. , vol.41 , pp. 334-341
    • Kathiresan, S.1    Voight, B.F.2    Purcell, S.3    Musunuru, K.4    Ardissino, D.5    Mannucci, P.M.6    Anand, S.7    Engert, J.C.8    Samani, N.J.9    Schunkert, H.10
  • 15
    • 57749209868 scopus 로고    scopus 로고
    • Crystal structures of protein phosphatase-1 bound to nodularin-R and tautomycin: a novel scaffold for structure-based drug design of serine/threonine phosphatase inhibitors
    • Kelker, M. S., Page, R. and Peti, W. (2009). Crystal structures of protein phosphatase-1 bound to nodularin-R and tautomycin: a novel scaffold for structure-based drug design of serine/threonine phosphatase inhibitors. J. Mol. Biol. 385, 11-21.
    • (2009) J. Mol. Biol. , vol.385 , pp. 11-21
    • Kelker, M.S.1    Page, R.2    Peti, W.3
  • 16
    • 34347232361 scopus 로고    scopus 로고
    • Phactr4 regulates neural tube and optic fissure closure by controlling PP1-, Rb-, and E2F1-regulated cell-cycle progression
    • Kim, T. H., Goodman, J., Anderson, K. V. and Niswander, L. (2007). Phactr4 regulates neural tube and optic fissure closure by controlling PP1-, Rb-, and E2F1-regulated cell-cycle progression. Dev. Cell 13, 87-102.
    • (2007) Dev. Cell , vol.13 , pp. 87-102
    • Kim, T.H.1    Goodman, J.2    Anderson, K.V.3    Niswander, L.4
  • 18
    • 52349088165 scopus 로고    scopus 로고
    • Myosin phosphatase interacts with and dephosphorylates the retinoblastoma protein in THP-1 leukemic cells: its inhibition is involved in the attenuation of daunorubicin-induced cell death by calyculin-A
    • Kiss, A., Lontay, B., Bécsi, B., Márkász, L., Oláh, E., Gergely, P. and Erdodi, F. (2008). Myosin phosphatase interacts with and dephosphorylates the retinoblastoma protein in THP-1 leukemic cells: its inhibition is involved in the attenuation of daunorubicin-induced cell death by calyculin-A. Cell. Signal. 20, 2059-2070.
    • (2008) Cell. Signal. , vol.20 , pp. 2059-2070
    • Kiss, A.1    Lontay, B.2    Bécsi, B.3    Márkász, L.4    Oláh, E.5    Gergely, P.6    Erdodi, F.7
  • 19
    • 63949087383 scopus 로고    scopus 로고
    • Molecular classification of melanomas and nevi using gene expression microarray signatures and formalin-fixed and paraffin-embedded tissue
    • Koh, S. S., Opel, M. L., Wei, J. P., Yau, K., Shah, R., Gorre, M. E., Whitman, E., Shitabata, P. K., Tao, Y., Cochran, A. J. et al. (2009). Molecular classification of melanomas and nevi using gene expression microarray signatures and formalin-fixed and paraffin-embedded tissue. Mod. Pathol. 22, 538-546.
    • (2009) Mod. Pathol. , vol.22 , pp. 538-546
    • Koh, S.S.1    Opel, M.L.2    Wei, J.P.3    Yau, K.4    Shah, R.5    Gorre, M.E.6    Whitman, E.7    Shitabata, P.K.8    Tao, Y.9    Cochran, A.J.10
  • 21
    • 0029789678 scopus 로고    scopus 로고
    • The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton
    • Leung, T., Chen, X. Q., Manser, E. and Lim, L. (1996). The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol. Cell. Biol. 16, 5313-5327.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5313-5327
    • Leung, T.1    Chen, X.Q.2    Manser, E.3    Lim, L.4
  • 22
    • 61849140657 scopus 로고    scopus 로고
    • Myocardin-related transcription factors and SRF are required for cytoskeletal dynamics and experimental metastasis
    • Medjkane, S., Perez-Sanchez, C., Gaggioli, C., Sahai, E. and Treisman, R. (2009). Myocardin-related transcription factors and SRF are required for cytoskeletal dynamics and experimental metastasis. Nat. Cell Biol. 11, 257-268.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 257-268
    • Medjkane, S.1    Perez-Sanchez, C.2    Gaggioli, C.3    Sahai, E.4    Treisman, R.5
  • 23
    • 0038737042 scopus 로고    scopus 로고
    • Actin dynamics control SRF activity by regulation of its coactivator MAL
    • Miralles, F., Posern, G., Zaromytidou, A. I. and Treisman, R. (2003). Actin dynamics control SRF activity by regulation of its coactivator MAL. Cell 113, 329-342.
    • (2003) Cell , vol.113 , pp. 329-342
    • Miralles, F.1    Posern, G.2    Zaromytidou, A.I.3    Treisman, R.4
  • 24
    • 57149087850 scopus 로고    scopus 로고
    • Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL
    • Mouilleron, S., Guettler, S., Langer, C. A., Treisman, R. and McDonald, N. Q. (2008). Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. EMBO J. 27, 3198-3208.
    • (2008) EMBO J , vol.27 , pp. 3198-3208
    • Mouilleron, S.1    Guettler, S.2    Langer, C.A.3    Treisman, R.4    McDonald, N.Q.5
  • 25
    • 79959259657 scopus 로고    scopus 로고
    • Structure of a pentavalent G-actin*MRTF-A complex reveals how G-actin controls nucleocytoplasmic shuttling of a transcriptional coactivator
    • Mouilleron, S., Langer, C. A., Guettler, S., McDonald, N. Q. and Treisman, R. (2011). Structure of a pentavalent G-actin*MRTF-A complex reveals how G-actin controls nucleocytoplasmic shuttling of a transcriptional coactivator. Sci. Signal. 4, ra40.
    • (2011) Sci. Signal. , vol.4
    • Mouilleron, S.1    Langer, C.A.2    Guettler, S.3    McDonald, N.Q.4    Treisman, R.5
  • 26
    • 84868558022 scopus 로고    scopus 로고
    • Structures of the Phactr1 RPEL domain and RPEL motif complexes with Gactin reveal the molecular basis for actin binding cooperativity
    • Mouilleron, S., Wiezlak, M., O'Reilly, N., Treisman, R. and McDonald, N. Q. (2012). Structures of the Phactr1 RPEL domain and RPEL motif complexes with Gactin reveal the molecular basis for actin binding cooperativity. Structure 20, 1960-1970.
    • (2012) Structure , vol.20 , pp. 1960-1970
    • Mouilleron, S.1    Wiezlak, M.2    O'Reilly, N.3    Treisman, R.4    McDonald, N.Q.5
  • 27
  • 28
    • 68549122708 scopus 로고    scopus 로고
    • Rho signaling, ROCK and mDia1, in transformation, metastasis and invasion
    • Narumiya, S., Tanji, M. and Ishizaki, T. (2009). Rho signaling, ROCK and mDia1, in transformation, metastasis and invasion. Cancer Metastasis Rev. 28, 65-76.
    • (2009) Cancer Metastasis Rev , vol.28 , pp. 65-76
    • Narumiya, S.1    Tanji, M.2    Ishizaki, T.3
  • 29
    • 77951582061 scopus 로고    scopus 로고
    • Linking actin dynamics and gene transcription to drive cellular motile functions
    • Olson, E. N. and Nordheim, A. (2010). Linking actin dynamics and gene transcription to drive cellular motile functions. Nat. Rev. Mol. Cell Biol. 11, 353-365.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 353-365
    • Olson, E.N.1    Nordheim, A.2
  • 30
    • 77958464695 scopus 로고    scopus 로고
    • An actin-regulated importin a/b-dependent extended bipartite NLS directs nuclear import of MRTF-A
    • Pawlowski, R., Rajakylä, E. K., Vartiainen, M. K. and Treisman, R. (2010). An actin-regulated importin a/b-dependent extended bipartite NLS directs nuclear import of MRTF-A. EMBO J. 29, 3448-3458.
    • (2010) EMBO J , vol.29 , pp. 3448-3458
    • Pawlowski, R.1    Rajakylä, E.K.2    Vartiainen, M.K.3    Treisman, R.4
  • 31
    • 0036906627 scopus 로고    scopus 로고
    • Mutant actins demonstrate a role for unpolymerized actin in control of transcription by serum response factor
    • Posern, G., Sotiropoulos, A. and Treisman, R. (2002). Mutant actins demonstrate a role for unpolymerized actin in control of transcription by serum response factor. Mol. Biol. Cell 13, 4167-4178.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4167-4178
    • Posern, G.1    Sotiropoulos, A.2    Treisman, R.3
  • 33
    • 77449110096 scopus 로고    scopus 로고
    • Cracking the phosphatase code: docking interactions determine substrate specificity
    • Roy, J. and Cyert, M. S. (2009). Cracking the phosphatase code: docking interactions determine substrate specificity. Sci. Signal. 2, re9.
    • (2009) Sci. Signal. , vol.2
    • Roy, J.1    Cyert, M.S.2
  • 35
    • 64149117979 scopus 로고    scopus 로고
    • Scapinin, the protein phosphatase 1 binding protein, enhances cell spreading and motility by interacting with the actin cytoskeleton
    • Sagara, J., Arata, T. and Taniguchi, S. (2009). Scapinin, the protein phosphatase 1 binding protein, enhances cell spreading and motility by interacting with the actin cytoskeleton. PLoS ONE 4, e4247.
    • (2009) PLoS ONE , vol.4
    • Sagara, J.1    Arata, T.2    Taniguchi, S.3
  • 37
    • 0032473351 scopus 로고    scopus 로고
    • RhoA effector mutants reveal distinct effector pathways for cytoskeletal reorganization, SRF activation and transformation
    • Sahai, E., Alberts, A. S. and Treisman, R. (1998). RhoA effector mutants reveal distinct effector pathways for cytoskeletal reorganization, SRF activation and transformation. EMBO J. 17, 1350-1361.
    • (1998) EMBO J , vol.17 , pp. 1350-1361
    • Sahai, E.1    Alberts, A.S.2    Treisman, R.3
  • 38
    • 27744600102 scopus 로고    scopus 로고
    • Whole-genome expression profiling of the melanoma progression pathway reveals marked molecular differences between nevi/ melanoma in situ and advanced-stage melanomas
    • Smith, A. P., Hoek, K. and Becker, D. (2005). Whole-genome expression profiling of the melanoma progression pathway reveals marked molecular differences between nevi/ melanoma in situ and advanced-stage melanomas. Cancer Biol. Ther. 4, 1018-1029.
    • (2005) Cancer Biol. Ther. , vol.4 , pp. 1018-1029
    • Smith, A.P.1    Hoek, K.2    Becker, D.3
  • 39
    • 0141751697 scopus 로고    scopus 로고
    • 2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases, and myosin phosphatase
    • 2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases, and myosin phosphatase. Physiol. Rev. 83, 1325-1358.
    • (2003) Physiol. Rev. , vol.83 , pp. 1325-1358
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 40
    • 0033597825 scopus 로고    scopus 로고
    • Signal-regulated activation of serum response factor is mediated by changes in actin dynamics
    • Sotiropoulos, A., Gineitis, D., Copeland, J. and Treisman, R. (1999). Signal-regulated activation of serum response factor is mediated by changes in actin dynamics. Cell 98, 159-169.
    • (1999) Cell , vol.98 , pp. 159-169
    • Sotiropoulos, A.1    Gineitis, D.2    Copeland, J.3    Treisman, R.4
  • 41
    • 79952352658 scopus 로고    scopus 로고
    • Dynamics of the Rho-family small GTPases in actin regulation and motility
    • Spiering, D. and Hodgson, L. (2011). Dynamics of the Rho-family small GTPases in actin regulation and motility. Cell Adh. Migr. 5, 170-180.
    • (2011) Cell Adh. Migr. , vol.5 , pp. 170-180
    • Spiering, D.1    Hodgson, L.2
  • 42
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction, I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J. A. and Watt, S. (1971). The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246, 4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 44
    • 34250849566 scopus 로고    scopus 로고
    • Nuclear actin regulates dynamic subcellular localization and activity of the SRF cofactor MAL
    • Vartiainen, M. K., Guettler, S., Larijani, B. and Treisman, R. (2007). Nuclear actin regulates dynamic subcellular localization and activity of the SRF cofactor MAL. Science 316, 1749-1752.
    • (2007) Science , vol.316 , pp. 1749-1752
    • Vartiainen, M.K.1    Guettler, S.2    Larijani, B.3    Treisman, R.4
  • 46
    • 33746562929 scopus 로고    scopus 로고
    • ROCK- and myosin-dependent matrix deformation enables protease-independent tumor-cell invasion in vivo
    • Wyckoff, J. B., Pinner, S. E., Gschmeissner, S., Condeelis, J. S. and Sahai, E. (2006). ROCK- and myosin-dependent matrix deformation enables protease-independent tumor-cell invasion in vivo. Curr. Biol. 16, 1515-1523.
    • (2006) Curr. Biol. , vol.16 , pp. 1515-1523
    • Wyckoff, J.B.1    Pinner, S.E.2    Gschmeissner, S.3    Condeelis, J.S.4    Sahai, E.5
  • 47
    • 84855303522 scopus 로고    scopus 로고
    • Phactr4 regulates directional migration of enteric neural crest through PP1, integrin signaling, and cofilin activity
    • Zhang, Y., Kim, T. H. and Niswander, L. (2012). Phactr4 regulates directional migration of enteric neural crest through PP1, integrin signaling, and cofilin activity. Genes Dev. 26, 69-81.
    • (2012) Genes Dev , vol.26 , pp. 69-81
    • Zhang, Y.1    Kim, T.H.2    Niswander, L.3
  • 48
    • 65349161753 scopus 로고    scopus 로고
    • Nuclear actin and actin-binding proteins in the regulation of transcription and gene expression
    • Zheng, B., Han, M., Bernier, M. and Wen, J. K. (2009). Nuclear actin and actin-binding proteins in the regulation of transcription and gene expression. FEBS J. 276, 2669-2685.
    • (2009) FEBS J , vol.276 , pp. 2669-2685
    • Zheng, B.1    Han, M.2    Bernier, M.3    Wen, J.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.