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Volumn 467, Issue 2, 2015, Pages 293-302

Functional cross-talk between Cdc42 and two downstream targets, Par6B and PAK4

Author keywords

Apical junction; Cell division cycle 42 (Cdc42); GTPase signalling; Kinase substrate; P21 protein (Cdc42 Rac) activated kinase 4 (PAK4); Partitioning defective 6 homologue (Par6)

Indexed keywords

P21 ACTIVATED KINASE 4; PARTITIONING DEFECTIVE 6B; PROTEIN CDC42; SCAFFOLD PROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; CDC42 PROTEIN, MOUSE; P21 ACTIVATED KINASE; PAK4 PROTEIN, HUMAN; PAK4 PROTEIN, MOUSE; PAR6B PROTEIN, HUMAN; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 84930009083     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20141352     Document Type: Article
Times cited : (22)

References (54)
  • 1
    • 0024235479 scopus 로고
    • The cellular basis of epithelial morphogenesis
    • Fristrom, D. (1988) The cellular basis of epithelial morphogenesis. A review. Tissue Cell 20, 645-690
    • (1988) A Review. Tissue Cell , vol.20 , pp. 645-690
    • Fristrom, D.1
  • 2
    • 0036439238 scopus 로고    scopus 로고
    • Molecular mechanisms of epithelial morphogenesis
    • Schock, F. and Perrimon, N. (2002) Molecular mechanisms of epithelial morphogenesis. Annu. Rev. Cell Dev. Biol. 18, 463-493
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 463-493
    • Schock, F.1    Perrimon, N.2
  • 3
    • 0024284814 scopus 로고
    • Identification of genes required for cytoplasmic localization in early C. Elegans embryos
    • Kemphues, K. J., Priess, J. R., Morton, D. G. and Cheng, N. S. (1988) Identification of genes required for cytoplasmic localization in early C. elegans embryos. Cell 52, 311-320
    • (1988) Cell , vol.52 , pp. 311-320
    • Kemphues, K.J.1    Priess, J.R.2    Morton, D.G.3    Cheng, N.S.4
  • 4
    • 0031674842 scopus 로고    scopus 로고
    • Atypical protein kinase C cooperates with PAR-3 to establish embryonic polarity in Caenorhabditis elegans
    • Tabuse, Y., Izumi, Y., Piano, F., Kemphues, K. J., Miwa, J. and Ohno, S. (1998) Atypical protein kinase C cooperates with PAR-3 to establish embryonic polarity in Caenorhabditis elegans. Development 125, 3607-3614 PubMed
    • (1998) Development , vol.125 , pp. 3607-3614
    • Tabuse, Y.1    Izumi, Y.2    Piano, F.3    Kemphues, K.J.4    Miwa, J.5    Ohno, S.6
  • 5
    • 34250134008 scopus 로고
    • Mutations affecting the pattern of the larval cuticle in Drosophila melanogaster - II. Zygotic loci on the third chromosome
    • Jürgens, G., Wieschaus, E., Nüsslein-Volhard, C. and Kluding, H. (1984) Mutations affecting the pattern of the larval cuticle in Drosophila melanogaster - II. Zygotic loci on the third chromosome. Wilhelm Roux's Arch. Dev. Biol. 193, 283-295
    • (1984) Wilhelm Roux's Arch. Dev. Biol. , vol.193 , pp. 283-295
    • Jürgens, G.1    Wieschaus, E.2    Nüsslein-Volhard, C.3    Kluding, H.4
  • 6
    • 0025285657 scopus 로고
    • Crumbs encodes an EGF-like protein expressed on apical membranes of Drosophila epithelial cells and required for organization of epithelia
    • Tepass, U., Theres, C. and Knust, E. (1990) crumbs encodes an EGF-like protein expressed on apical membranes of Drosophila epithelial cells and required for organization of epithelia. Cell 61, 787-799
    • (1990) Cell , vol.61 , pp. 787-799
    • Tepass, U.1    Theres, C.2    Knust, E.3
  • 7
    • 0033582916 scopus 로고    scopus 로고
    • Discs lost, a novel multi-PDZ domain protein, establishes and maintains epithelial polarity
    • Bhat, M. A., Izaddoost, S., Lu, Y., Cho, K. O., Choi, K. W. and Bellen, H. J. (1999) Discs lost, a novel multi-PDZ domain protein, establishes and maintains epithelial polarity. Cell 96, 833-845
    • (1999) Cell , vol.96 , pp. 833-845
    • Bhat, M.A.1    Izaddoost, S.2    Lu, Y.3    Cho, K.O.4    Choi, K.W.5    Bellen, H.J.6
  • 8
    • 0346624902 scopus 로고    scopus 로고
    • The Drosophila cell survival gene discs lost encodes a cytoplasmic Codanin-1-like protein, not a homolog of tight junction PDZ protein Patj
    • Pielage, J., Stork, T., Bunse, I. and Klämbt, C. (2003) The Drosophila cell survival gene discs lost encodes a cytoplasmic Codanin-1-like protein, not a homolog of tight junction PDZ protein Patj. Dev. Cell 5, 841-851
    • (2003) Dev. Cell , vol.5 , pp. 841-851
    • Pielage, J.1    Stork, T.2    Bunse, I.3    Klämbt, C.4
  • 9
    • 33646889804 scopus 로고    scopus 로고
    • Domain-specific early and late function of Dpatj in Drosophila photoreceptor cells
    • Nam, S. C. and Choi, K. W. (2006) Domain-specific early and late function of Dpatj in Drosophila photoreceptor cells. Dev. Dyn. 235, 1501-1507
    • (2006) Dev. Dyn. , vol.235 , pp. 1501-1507
    • Nam, S.C.1    Choi, K.W.2
  • 10
    • 0034628471 scopus 로고    scopus 로고
    • Localization of apical epithelial determinants by the basolateral PDZ protein Scribble
    • Bilder, D. and Perrimon, N. (2000) Localization of apical epithelial determinants by the basolateral PDZ protein Scribble. Nature 403, 676-680
    • (2000) Nature , vol.403 , pp. 676-680
    • Bilder, D.1    Perrimon, N.2
  • 11
    • 0034617129 scopus 로고    scopus 로고
    • Cooperative regulation of cell polarity and growth by Drosophila tumor suppressors
    • Bilder, D., Li, M. and Perrimon, N. (2000) Cooperative regulation of cell polarity and growth by Drosophila tumor suppressors. Science 289, 113-116
    • (2000) Science , vol.289 , pp. 113-116
    • Bilder, D.1    Li, M.2    Perrimon, N.3
  • 12
    • 0034253536 scopus 로고    scopus 로고
    • The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42
    • Joberty, G., Petersen, C., Gao, L. and Macara, I. G. G. (2000) The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42. Nat. Cell Biol. 2, 531-539
    • (2000) Nat. Cell Biol. , vol.2 , pp. 531-539
    • Joberty, G.1    Petersen, C.2    Gao, L.3    Macara, I.G.G.4
  • 13
    • 84870221288 scopus 로고    scopus 로고
    • The apical polarity protein network in Drosophila epithelial cells: Regulation of polarity, junctions, morphogenesis, cell growth, and survival
    • Tepass, U. (2012) The apical polarity protein network in Drosophila epithelial cells: regulation of polarity, junctions, morphogenesis, cell growth, and survival. Annu. Rev. Cell Dev. Biol. 28, 655-685
    • (2012) Annu. Rev. Cell Dev. Biol. , vol.28 , pp. 655-685
    • Tepass, U.1
  • 14
    • 77955501804 scopus 로고    scopus 로고
    • Widely conserved signaling pathways in the establishment of cell polarity
    • McCaffrey, L. M. and Macara, I. G. (2009) Widely conserved signaling pathways in the establishment of cell polarity. Cold Spring Harb. Perspect. Biol. 1, a001370
    • (2009) Cold Spring Harb. Perspect. Biol. , vol.1 , pp. a001370
    • McCaffrey, L.M.1    Macara, I.G.2
  • 16
    • 33751347857 scopus 로고    scopus 로고
    • The Scribble and Par complexes in polarity and migration: Friends or foes?
    • Humbert, P. O., Dow, L. E. and Russell, S. M. (2006) The Scribble and Par complexes in polarity and migration: friends or foes? Trends Cell Biol. 16, 622-630
    • (2006) Trends Cell Biol. , vol.16 , pp. 622-630
    • Humbert, P.O.1    Dow, L.E.2    Russell, S.M.3
  • 17
    • 0037225708 scopus 로고    scopus 로고
    • Interactions between the crumbs, lethal giant larvae and bazooka pathways in epithelial polarization
    • Tanentzapf, G. and Tepass, U. (2003) Interactions between the crumbs, lethal giant larvae and bazooka pathways in epithelial polarization. Nat. Cell Biol. 5, 46-52
    • (2003) Nat. Cell Biol. , vol.5 , pp. 46-52
    • Tanentzapf, G.1    Tepass, U.2
  • 18
  • 22
    • 84912092373 scopus 로고    scopus 로고
    • Architecture of tight junctions and principles of molecular composition
    • Van Itallie, C. M. and Anderson, J. M. (2014) Architecture of tight junctions and principles of molecular composition. Semin. Cell Dev. Biol. 36, 1-9
    • (2014) Semin. Cell Dev. Biol. , vol.36 , pp. 1-9
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 23
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville, S. and Hall, A. (2002) Rho GTPases in cell biology. Nature 420, 629-635
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 24
    • 0035313804 scopus 로고    scopus 로고
    • Multiple roles for Cdc42 in cell regulation
    • Erickson, J. W. and Cerione, R. A. (2001) Multiple roles for Cdc42 in cell regulation. Curr. Opin. Cell Biol. 13, 153-157
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 153-157
    • Erickson, J.W.1    Cerione, R.A.2
  • 25
    • 34547571737 scopus 로고    scopus 로고
    • Localized zones of Rho and Rac activities drive initiation and expansion of epithelial cell-cell adhesion
    • Yamada, S. and Nelson, W. J. (2007) Localized zones of Rho and Rac activities drive initiation and expansion of epithelial cell-cell adhesion. J. Cell Biol. 178, 517-527
    • (2007) J. Cell Biol. , vol.178 , pp. 517-527
    • Yamada, S.1    Nelson, W.J.2
  • 26
    • 13444252631 scopus 로고    scopus 로고
    • GEF means go: Turning on RHO GTPases with guanine nucleotide-exchange factors
    • Rossman, K. L., Der, C. J. and Sondek, J. (2005) GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors. Nat. Rev. Mol. Cell Biol. 6, 167-180
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 167-180
    • Rossman, K.L.1    Der, C.J.2    Sondek, J.3
  • 27
    • 33846969965 scopus 로고    scopus 로고
    • Current knowledge of the large RhoGAP family of proteins
    • Tcherkezian, J. and Lamarche-Vane, N. (2007) Current knowledge of the large RhoGAP family of proteins. Biol. Cell 99, 67-86
    • (2007) Biol. Cell , vol.99 , pp. 67-86
    • Tcherkezian, J.1    Lamarche-Vane, N.2
  • 28
    • 78751692389 scopus 로고    scopus 로고
    • The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells
    • Wallace, S. W., Magalhaes, A. and Hall, A. (2011) The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells. Mol. Cell. Biol. 31, 81-91
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 81-91
    • Wallace, S.W.1    Magalhaes, A.2    Hall, A.3
  • 29
    • 77956247092 scopus 로고    scopus 로고
    • Cdc42 regulates apical junction formation in human bronchial epithelial cells through PAK4 and Par6B
    • Wallace, S. W., Durgan, J., Jin, D. and Hall, A. (2010) Cdc42 regulates apical junction formation in human bronchial epithelial cells through PAK4 and Par6B. Mol. Biol. Cell 21, 2996-3006
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2996-3006
    • Wallace, S.W.1    Durgan, J.2    Jin, D.3    Hall, A.4
  • 30
    • 84863299837 scopus 로고    scopus 로고
    • Group I and II mammalian PAKs have different modes of activation by Cdc42
    • Baskaran, Y., Ng, Y.-W., Selamat, W., Ling, F. T. P. and Manser, E. (2012) Group I and II mammalian PAKs have different modes of activation by Cdc42. EMBO Rep. 13, 653-659
    • (2012) EMBO Rep. , vol.13 , pp. 653-659
    • Baskaran, Y.1    Ng, Y.-W.2    Selamat, W.3    Ling, F.T.P.4    Manser, E.5
  • 31
    • 0031948850 scopus 로고    scopus 로고
    • A conserved negative regulatory region in alphaPAK: Inhibition of PAK kinases reveals their morphological roles downstream of Cdc42 and Rac1
    • Zhao, Z. S., Manser, E., Chen, X. Q., Chong, C., Leung, T. and Lim, L. (1998) A conserved negative regulatory region in alphaPAK: inhibition of PAK kinases reveals their morphological roles downstream of Cdc42 and Rac1. Mol. Cell. Biol. 18, 2153-2163 PubMed
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2153-2163
    • Zhao, Z.S.1    Manser, E.2    Chen, X.Q.3    Chong, C.4    Leung, T.5    Lim, L.6
  • 33
    • 2942626082 scopus 로고    scopus 로고
    • Sequential roles of Cdc42, Par-6, aPKC, and Lgl in the establishment of epithelial polarity during Drosophila embryogenesis
    • Hutterer, A., Betschinger, J., Petronczki, M. and Knoblich, J. A. (2004) Sequential roles of Cdc42, Par-6, aPKC, and Lgl in the establishment of epithelial polarity during Drosophila embryogenesis. Dev. Cell 6, 845-854
    • (2004) Dev. Cell , vol.6 , pp. 845-854
    • Hutterer, A.1    Betschinger, J.2    Petronczki, M.3    Knoblich, J.A.4
  • 34
    • 0034659420 scopus 로고    scopus 로고
    • A human homolog of the C. Elegans polarity determinant Par-6 links Rac and Cdc42 to PKC ζ signaling and cell transformation
    • Qiu, R.-G., Abo, A. and Martin, G. S. S. (2000) A human homolog of the C. elegans polarity determinant Par-6 links Rac and Cdc42 to PKC ζ signaling and cell transformation. Curr. Biol. 10, 697-707
    • (2000) Curr. Biol. , vol.10 , pp. 697-707
    • Qiu, R.-G.1    Abo, A.2    Martin, G.S.S.3
  • 35
    • 0000202186 scopus 로고    scopus 로고
    • A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity
    • Lin, D., Edwards, A. S. S., Fawcett, J. P. P., Mbamalu, G., Scott, J. D. D. and Pawson, T. (2000) A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity. Nat. Cell Biol. 2, 540-547
    • (2000) Nat. Cell Biol. , vol.2 , pp. 540-547
    • Lin, D.1    Edwards, A.S.S.2    Fawcett, J.P.P.3    Mbamalu, G.4    Scott, J.D.D.5    Pawson, T.6
  • 36
    • 0037416217 scopus 로고    scopus 로고
    • Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6
    • Garrard, S. M. S. M., Capaldo, C. T. C. T., Gao, L., Rosen, M. K. M. K., Macara, I. G. I. G. and Tomchick, D. R. D. R. (2003) Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6. EMBO J. 22, 1125-1133
    • (2003) EMBO J. , vol.22 , pp. 1125-1133
    • Garrard, S.M.S.M.1    Capaldo, C.T.C.T.2    Gao, L.3    Rosen, M.K.M.K.4    Macara, I.G.I.G.5    Tomchick, D.R.D.R.6
  • 37
    • 1642276423 scopus 로고    scopus 로고
    • Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIB-PDZ transition
    • Peterson, F. C., Penkert, R. R., Volkman, B. F. and Prehoda, K. E. (2004) Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIB-PDZ transition. Mol. Cell 13, 665-676
    • (2004) Mol. Cell , vol.13 , pp. 665-676
    • Peterson, F.C.1    Penkert, R.R.2    Volkman, B.F.3    Prehoda, K.E.4
  • 38
    • 84862281704 scopus 로고    scopus 로고
    • Partitioning-defective protein 6 (Par-6) activates atypical protein kinase C (aPKC) by pseudosubstrate displacement
    • Graybill, C., Wee, B., Atwood, S. X. and Prehoda, K. E. (2012) Partitioning-defective protein 6 (Par-6) activates atypical protein kinase C (aPKC) by pseudosubstrate displacement. J. Biol. Chem. 287, 21003-21011
    • (2012) J. Biol. Chem. , vol.287 , pp. 21003-21011
    • Graybill, C.1    Wee, B.2    Atwood, S.X.3    Prehoda, K.E.4
  • 39
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider, C. A., Rasband, W. S. and Eliceiri, K. W. (2012) NIH Image to ImageJ: 25 years of image analysis. Nat. Methods 9, 671-675
    • (2012) Nat. Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 40
    • 84856391412 scopus 로고    scopus 로고
    • Ubiquitination, localization, and stability of an anti-apoptotic BCL2-like protein, BCL2L10/BCLb, are regulated by Ubiquilin1
    • Beverly, L. J., Lockwood, W. W., Shah, P. P., Erdjument-Bromage, H. and Varmus, H. (2012) Ubiquitination, localization, and stability of an anti-apoptotic BCL2-like protein, BCL2L10/BCLb, are regulated by Ubiquilin1. Proc. Natl. Acad. Sci. U. S. A. 109, E119-E126
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. E119-E126
    • Beverly, L.J.1    Lockwood, W.W.2    Shah, P.P.3    Erdjument-Bromage, H.4    Varmus, H.5
  • 41
    • 33947256308 scopus 로고    scopus 로고
    • Docking interactions in protein kinase and phosphatase networks
    • Reményi, A., Good, M. C. and Lim, W. A. (2006) Docking interactions in protein kinase and phosphatase networks. Curr. Opin. Struct. Biol. 16, 676-685
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 676-685
    • Reményi, A.1    Good, M.C.2    Lim, W.A.3
  • 42
    • 0032538973 scopus 로고    scopus 로고
    • PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia
    • Abo, A., Qu, J., Cammarano, M. S. S., Dan, C., Fritsch, A., Baud, V., Belisle, B. and Minden, A. (1998) PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia. EMBO J. 17, 6527-6540
    • (1998) EMBO J. , vol.17 , pp. 6527-6540
    • Abo, A.1    Qu, J.2    Cammarano, M.S.S.3    Dan, C.4    Fritsch, A.5    Baud, V.6    Belisle, B.7    Minden, A.8
  • 43
    • 24144443830 scopus 로고    scopus 로고
    • The positioning and segregation of apical cues during epithelial polarity establishment in Drosophila
    • Harris, T. J. C. and Peifer, M. (2005) The positioning and segregation of apical cues during epithelial polarity establishment in Drosophila. J. Cell Biol. 170, 813-823
    • (2005) J. Cell Biol. , vol.170 , pp. 813-823
    • Harris, T.J.C.1    Peifer, M.2
  • 44
    • 0035141027 scopus 로고    scopus 로고
    • DmPAR-6 directs epithelial polarity and asymmetric cell division of neuroblasts in Drosophila
    • Petronczki, M. and Knoblich, J. A. (2001) DmPAR-6 directs epithelial polarity and asymmetric cell division of neuroblasts in Drosophila. Nat. Cell Biol. 3, 43-49
    • (2001) Nat. Cell Biol. , vol.3 , pp. 43-49
    • Petronczki, M.1    Knoblich, J.A.2
  • 45
    • 84874995825 scopus 로고    scopus 로고
    • The WD40 protein Morg1 facilitates Par6-aPKC binding to Crb3 for apical identity in epithelial cells
    • Hayase, J., Kamakura, S., Iwakiri, Y., Yamaguchi, Y., Izaki, T., Ito, T. and Sumimoto, H. (2013) The WD40 protein Morg1 facilitates Par6-aPKC binding to Crb3 for apical identity in epithelial cells. J. Cell Biol. 200, 635-650
    • (2013) J. Cell Biol. , vol.200 , pp. 635-650
    • Hayase, J.1    Kamakura, S.2    Iwakiri, Y.3    Yamaguchi, Y.4    Izaki, T.5    Ito, T.6    Sumimoto, H.7
  • 46
    • 33646485094 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites
    • Hoffert, J. D., Pisitkun, T., Wang, G., Shen, R. and Knepper, M. A. (2006) Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites. Proc. Natl. Acad. Sci. U. S. A. 103, 7159-7164
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 7159-7164
    • Hoffert, J.D.1    Pisitkun, T.2    Wang, G.3    Shen, R.4    Knepper, M.A.5
  • 47
    • 84876011758 scopus 로고    scopus 로고
    • PAK signaling in cancer
    • Ye, D. Z. and Field, J. (2012) PAK signaling in cancer. Cell. Logist. 2, 105-116
    • (2012) Cell. Logist. , vol.2 , pp. 105-116
    • Ye, D.Z.1    Field, J.2
  • 51
    • 70349591634 scopus 로고    scopus 로고
    • Identification of PAK4 as a putative target gene for amplification within 19q13.12-q13.2 in oral squamous-cell carcinoma
    • Begum, A., Imoto, I., Kozaki, K., Tsuda, H., Suzuki, E., Amagasa, T. and Inazawa, J. (2009) Identification of PAK4 as a putative target gene for amplification within 19q13.12-q13.2 in oral squamous-cell carcinoma. Cancer Sci. 100, 1908-1916
    • (2009) Cancer Sci. , vol.100 , pp. 1908-1916
    • Begum, A.1    Imoto, I.2    Kozaki, K.3    Tsuda, H.4    Suzuki, E.5    Amagasa, T.6    Inazawa, J.7
  • 52
    • 84866894408 scopus 로고    scopus 로고
    • Comprehensive genomic characterization of squamous cell lung cancers
    • The Cancer Genome Atlas Research Network (2012) Comprehensive genomic characterization of squamous cell lung cancers. Nature 489, 519-525
    • (2012) Nature , vol.489 , pp. 519-525
    • The Cancer Genome Atlas Research Network1
  • 53
    • 33646852807 scopus 로고    scopus 로고
    • The novel WD-repeat protein Morg1 acts as a molecular scaffold for hypoxia-inducible factor prolyl hydroxylase 3 (PHD3)
    • Hopfer, U., Hopfer, H., Jablonski, K., Stahl, R. A. K. and Wolf, G. (2006) The novel WD-repeat protein Morg1 acts as a molecular scaffold for hypoxia-inducible factor prolyl hydroxylase 3 (PHD3). J. Biol. Chem. 281, 8645-8655
    • (2006) J. Biol. Chem. , vol.281 , pp. 8645-8655
    • Hopfer, U.1    Hopfer, H.2    Jablonski, K.3    Stahl, R.A.K.4    Wolf, G.5
  • 54
    • 2342474379 scopus 로고    scopus 로고
    • Modular construction of a signaling scaffold: MORG1 interacts with components of the ERK cascade and links ERK signaling to specific agonists
    • Vomastek, T., Schaeffer, H.-J., Tarcsafalvi, A., Smolkin, M. E., Bissonette, E. A. and Weber, M. J. (2004) Modular construction of a signaling scaffold: MORG1 interacts with components of the ERK cascade and links ERK signaling to specific agonists. Proc. Natl. Acad. Sci. U. S. A. 101, 6981-6986
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 6981-6986
    • Vomastek, T.1    Schaeffer, H.-J.2    Tarcsafalvi, A.3    Smolkin, M.E.4    Bissonette, E.A.5    Weber, M.J.6


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