메뉴 건너뛰기




Volumn 289, Issue 37, 2014, Pages 25393-25403

Crystal structure of the cGMP-dependent protein kinase II leucine zipper and Rab11b protein complex reveals molecular details of G-kinase-specific interactions

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CROSSTALK; ENZYMES; TRANSCRIPTION FACTORS; VAN DER WAALS FORCES;

EID: 84907185231     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.575894     Document Type: Article
Times cited : (20)

References (44)
  • 2
    • 33644834949 scopus 로고    scopus 로고
    • Function of cGMP-dependent protein kinases as revealed by gene deletion
    • Hofmann, F., Feil, R., Kleppisch, T., and Schlossmann, J. (2006) Function of cGMP-dependent protein kinases as revealed by gene deletion. Physiol. Rev. 86, 1-23
    • (2006) Physiol. Rev , vol.86 , pp. 1-23
    • Hofmann, F.1    Feil, R.2    Kleppisch, T.3    Schlossmann, J.4
  • 3
    • 77956283047 scopus 로고    scopus 로고
    • CGMP-dependent protein kinases andcGMPphosphodiesterases in nitric oxide and cGMP action
    • Francis, S. H., Busch, J. L., Corbin, J. D., and Sibley, D. (2010) cGMP-dependent protein kinases andcGMPphosphodiesterases in nitric oxide and cGMP action. Pharmacol. Rev. 62, 525-563
    • (2010) Pharmacol. Rev , vol.62 , pp. 525-563
    • Francis, S.H.1    Busch, J.L.2    Corbin, J.D.3    Sibley, D.4
  • 4
    • 0031172791 scopus 로고    scopus 로고
    • Characterization of the human gene encoding the type Iα and type Iβ cGMP-dependent protein kinase (PRKG1)
    • Orstavik, S., Natarajan, V., Taskén, K., Jahnsen, T., and Sandberg, M. (1997) Characterization of the human gene encoding the type Iα and type Iβ cGMP-dependent protein kinase (PRKG1). Genomics 42, 311-318
    • (1997) Genomics , vol.42 , pp. 311-318
    • Orstavik, S.1    Natarajan, V.2    Taskén, K.3    Jahnsen, T.4    Sandberg, M.5
  • 5
    • 0024325064 scopus 로고
    • Molecular cloning and predicted full-length amino acid sequence of the type Iβ isozyme of cGMP-dependent protein kinase from human placenta. Tissue distribution and developmental changes in rat
    • Sandberg, M., Natarajan, V., Ronander, I., Kalderon, D., Walter, U., Lohmann, S. M., and Jahnsen, T. (1989) Molecular cloning and predicted full-length amino acid sequence of the type Iβ isozyme of cGMP-dependent protein kinase from human placenta. Tissue distribution and developmental changes in rat. FEBS Lett. 255, 321-329
    • (1989) FEBS Lett , vol.255 , pp. 321-329
    • Sandberg, M.1    Natarajan, V.2    Ronander, I.3    Kalderon, D.4    Walter, U.5    Lohmann, S.M.6    Jahnsen, T.7
  • 6
    • 0019363607 scopus 로고
    • Cyclic GMP-dependent protein kinase in intestinal brush borders
    • de Jonge, H. R. (1981) Cyclic GMP-dependent protein kinase in intestinal brush borders. Adv. Cyclic Nucleotide Res. 14, 315-333
    • (1981) Adv. Cyclic Nucleotide Res , vol.14 , pp. 315-333
    • De Jonge, H.R.1
  • 8
    • 0030452310 scopus 로고    scopus 로고
    • Intestinal secretory defects and dwarfism in mice lacking cGMPdependent protein kinase II
    • Pfeifer, A., Aszódi, A., Seidler, U., Ruth, P., Hofmann, F., and Fässler, R. (1996) Intestinal secretory defects and dwarfism in mice lacking cGMPdependent protein kinase II. Science 274, 2082-2086
    • (1996) Science , vol.274 , pp. 2082-2086
    • Pfeifer, A.1    Aszódi, A.2    Seidler, U.3    Ruth, P.4    Hofmann, F.5    Fässler, R.6
  • 10
    • 35148819200 scopus 로고    scopus 로고
    • Interactions between the leucine-zipper motif of cGMP-dependent protein kinase and the C-terminal region of the targeting subunit of myosin light chain phosphatase
    • Lee, E., Hayes, D. B., Langsetmo, K., Sundberg, E. J., and Tao, T. C. (2007) Interactions between the leucine-zipper motif of cGMP-dependent protein kinase and the C-terminal region of the targeting subunit of myosin light chain phosphatase. J. Mol. Biol. 373, 1198-1212
    • (2007) J. Mol. Biol , vol.373 , pp. 1198-1212
    • Lee, E.1    Hayes, D.B.2    Langsetmo, K.3    Sundberg, E.J.4    Tao, T.C.5
  • 12
    • 33644687046 scopus 로고    scopus 로고
    • Identification of the interface between cGMP-dependent protein kinase Iβ and its interaction partners TFII-I and IRAG reveals a common interaction motif
    • Casteel, D. E., Boss, G. R., and Pilz, R. B. (2005) Identification of the interface between cGMP-dependent protein kinase Iβ and its interaction partners TFII-I and IRAG reveals a common interaction motif. J. Biol. Chem. 280, 38211-38218
    • (2005) J. Biol. Chem , vol.280 , pp. 38211-38218
    • Casteel, D.E.1    Boss, G.R.2    Pilz, R.B.3
  • 13
    • 0028784412 scopus 로고
    • Isotype-specific activation of cystic fibrosis transmembrane conductance regulator-chloride channels by cGMP-dependent protein kinase II
    • French, P. J., Bijman, J., Edixhoven, M., Vaandrager, A. B., Scholte, B. J., Lohmann, S. M., Nairn, A. C., and de Jonge, H. R. (1995) Isotype-specific activation of cystic fibrosis transmembrane conductance regulator-chloride channels by cGMP-dependent protein kinase II. J. Biol. Chem. 270, 26626-26631
    • (1995) J. Biol. Chem , vol.270 , pp. 26626-26631
    • French, P.J.1    Bijman, J.2    Edixhoven, M.3    Vaandrager, A.B.4    Scholte, B.J.5    Lohmann, S.M.6    Nairn, A.C.7    De Jonge, H.R.8
  • 17
    • 0027934888 scopus 로고
    • Molecular analysis of mouse Rab11b: A new type of mammalian YPT/Rab protein
    • Lai, F., Stubbs, L., and Artzt, K. (1994) Molecular analysis of mouse Rab11b: a new type of mammalian YPT/Rab protein. Genomics 22, 610-616
    • (1994) Genomics , vol.22 , pp. 610-616
    • Lai, F.1    Stubbs, L.2    Artzt, K.3
  • 18
    • 0027160730 scopus 로고
    • Identification of a small GTP-binding protein, Rab25, expressed in the gastrointestinal mucosa, kidney, and lung
    • Goldenring, J. R., Shen, K. R., Vaughan, H. D., and Modlin, I. M. (1993) Identification of a small GTP-binding protein, Rab25, expressed in the gastrointestinal mucosa, kidney, and lung. J. Biol. Chem. 268, 18419-18422
    • (1993) J. Biol. Chem , vol.268 , pp. 18419-18422
    • Goldenring, J.R.1    Shen, K.R.2    Vaughan, H.D.3    Modlin, I.M.4
  • 19
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffic
    • Stenmark, H. (2009) Rab GTPases as coordinators of vesicle traffic. Nat. Rev. Mol. Cell Biol. 10, 513-525
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 20
    • 18144380651 scopus 로고    scopus 로고
    • Structural clues to Rab GTPase functional diversity
    • Pfeffer, S. R. (2005) Structural clues to Rab GTPase functional diversity. J. Biol. Chem. 280, 15485-15488
    • (2005) J. Biol. Chem , vol.280 , pp. 15485-15488
    • Pfeffer, S.R.1
  • 22
    • 33750365184 scopus 로고    scopus 로고
    • Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin- 1
    • Shiba, T., Koga, H., Shin, H. W., Kawasaki, M., Kato, R., Nakayama, K., and Wakatsuki, S. (2006) Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin- 1. Proc. Natl. Acad. Sci. U.S.A. 103, 15416-15421
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 15416-15421
    • Shiba, T.1    Koga, H.2    Shin, H.W.3    Kawasaki, M.4    Kato, R.5    Nakayama, K.6    Wakatsuki, S.7
  • 23
    • 4043181982 scopus 로고    scopus 로고
    • Molecular characterization of Rab11 interactions with members of the family of Rab11-interacting proteins
    • Junutula, J. R., Schonteich, E., Wilson, G. M., Peden, A. A., Scheller, R. H., and Prekeris, R. (2004) Molecular characterization of Rab11 interactions with members of the family of Rab11-interacting proteins. J. Biol. Chem. 279, 33430-33437
    • (2004) J. Biol. Chem , vol.279 , pp. 33430-33437
    • Junutula, J.R.1    Schonteich, E.2    Wilson, G.M.3    Peden, A.A.4    Scheller, R.H.5    Prekeris, R.6
  • 24
    • 33746846072 scopus 로고    scopus 로고
    • Crystal structure of rab11 in complex with rab11 family interacting protein 2
    • Jagoe, W. N., Lindsay, A. J., Read, R. J., McCoy, A. J., McCaffrey, M. W., and Khan, A. R. (2006) Crystal structure of rab11 in complex with rab11 family interacting protein 2. Structure 14, 1273-1283
    • (2006) Structure , vol.14 , pp. 1273-1283
    • Jagoe, W.N.1    Lindsay, A.J.2    Read, R.J.3    McCoy, A.J.4    McCaffrey, M.W.5    Khan, A.R.6
  • 25
    • 33750437407 scopus 로고    scopus 로고
    • Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes
    • Eathiraj, S., Mishra, A., Prekeris, R., and Lambright, D. G. (2006) Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes. J. Mol. Biol. 364, 121-135
    • (2006) J. Mol. Biol , vol.364 , pp. 121-135
    • Eathiraj, S.1    Mishra, A.2    Prekeris, R.3    Lambright, D.G.4
  • 26
    • 48849093476 scopus 로고    scopus 로고
    • Trafficking of cGMP-dependent protein kinase II via interaction with Rab11
    • Yuasa, K., Yamagami, S., Nagahama, M., and Tsuji, A. (2008) Trafficking of cGMP-dependent protein kinase II via interaction with Rab11. Biochem. Biophys. Res. Commun. 374, 522-526
    • (2008) Biochem. Biophys. Res. Commun , vol.374 , pp. 522-526
    • Yuasa, K.1    Yamagami, S.2    Nagahama, M.3    Tsuji, A.4
  • 27
    • 59849102081 scopus 로고    scopus 로고
    • Rab11 regulates the recycling of the β2-adrenergic receptor through a direct interaction
    • Parent, A., Hamelin, E., Germain, P., and Parent, J. L. (2009) Rab11 regulates the recycling of the β2-adrenergic receptor through a direct interaction. Biochem. J. 418, 163-172
    • (2009) Biochem. J , vol.418 , pp. 163-172
    • Parent, A.1    Hamelin, E.2    Germain, P.3    Parent, J.L.4
  • 28
    • 33645222317 scopus 로고    scopus 로고
    • Direct interaction with Rab11a targets the epithelial Ca2+ channels TRPV5 and TRPV6 to the plasma membrane
    • van de Graaf, S. F., Chang, Q., Mensenkamp, A. R., Hoenderop, J. G., and Bindels, R. J. (2006) Direct interaction with Rab11a targets the epithelial Ca2+ channels TRPV5 and TRPV6 to the plasma membrane. Mol. Cell. Biol. 26, 303-312
    • (2006) Mol. Cell. Biol , vol.26 , pp. 303-312
    • Van De Graaf, S.F.1    Chang, Q.2    Mensenkamp, A.R.3    Hoenderop, J.G.4    Bindels, R.J.5
  • 29
    • 27744469168 scopus 로고    scopus 로고
    • The intracellular trafficking of the G protein-coupled receptor TPβ depends on a direct interaction with Rab11
    • Hamelin, E., Thériault, C., Laroche, G., and Parent, J. L. (2005) The intracellular trafficking of the G protein-coupled receptor TPβ depends on a direct interaction with Rab11. J. Biol. Chem. 280, 36195-36205
    • (2005) J. Biol. Chem , vol.280 , pp. 36195-36205
    • Hamelin, E.1    Thériault, C.2    Laroche, G.3    Parent, J.L.4
  • 30
    • 84877969744 scopus 로고    scopus 로고
    • BDNF-dependent recycling facilitates TrkB translocation to postsynaptic density during LTP via a Rab11-dependent pathway
    • Huang, S. H., Wang, J., Sui, W. H., Chen, B., Zhang, X. Y., Yan, J., Geng, Z., and Chen, Z. Y. (2013) BDNF-dependent recycling facilitates TrkB translocation to postsynaptic density during LTP via a Rab11-dependent pathway. J. Neurosci. 33, 9214-9230
    • (2013) J. Neurosci , vol.33 , pp. 9214-9230
    • Huang, S.H.1    Wang, J.2    Sui, W.H.3    Chen, B.4    Zhang, X.Y.5    Yan, J.6    Geng, Z.7    Chen, Z.Y.8
  • 32
    • 84877972950 scopus 로고    scopus 로고
    • CGMP-dependent protein kinase Iβ regulates breast cancer cell migration and invasion via interaction with the actin/myosinassociated protein caldesmon
    • Schwappacher, R., Rangaswami, H., Su-Yuo, J., Hassad, A., Spitler, R., and Casteel, D. E. (2013) cGMP-dependent protein kinase Iβ regulates breast cancer cell migration and invasion via interaction with the actin/myosinassociated protein caldesmon. J. Cell Sci. 126, 1626-1636
    • (2013) J. Cell Sci , vol.126 , pp. 1626-1636
    • Schwappacher, R.1    Rangaswami, H.2    Su-Yuo, J.3    Hassad, A.4    Spitler, R.5    Casteel, D.E.6
  • 34
  • 36
    • 33646701199 scopus 로고    scopus 로고
    • The crystal structure of the small GTPase Rab11b reveals critical differences relative to the Rab11a isoform
    • Scapin, S. M., Carneiro, F. R., Alves, A. C., Medrano, F. J., Guimarães, B. G., and Zanchin, N. I. (2006) The crystal structure of the small GTPase Rab11b reveals critical differences relative to the Rab11a isoform. J. Struct. Biol. 154, 260-268
    • (2006) J. Struct. Biol , vol.154 , pp. 260-268
    • Scapin, S.M.1    Carneiro, F.R.2    Alves, A.C.3    Medrano, F.J.4    Guimarães, B.G.5    Zanchin, N.I.6
  • 38
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M. D., Isupov, M. N., and Murshudov, G. N. (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D Biol. Crystallogr. 57, 122-133
    • (2001) Acta Crystallogr. D Biol. Crystallogr , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 39
    • 0032102906 scopus 로고    scopus 로고
    • Computational approaches to identify leucine zippers
    • Bornberg-Bauer, E., Rivals, E., and Vingron, M. (1998) Computational approaches to identify leucine zippers. Nucleic Acids Res. 26, 2740-2746
    • (1998) Nucleic Acids Res , vol.26 , pp. 2740-2746
    • Bornberg-Bauer, E.1    Rivals, E.2    Vingron, M.3
  • 40
    • 77958510993 scopus 로고    scopus 로고
    • A crystal structure of the cyclic GMP-dependent protein kinase Iβ dimerization/docking domain reveals molecular details of isoform- specific anchoring
    • Casteel, D. E., Smith-Nguyen, E. V., Sankaran, B., Roh, S. H., Pilz, R. B., and Kim, C. (2010) A crystal structure of the cyclic GMP-dependent protein kinase Iβ dimerization/docking domain reveals molecular details of isoform- specific anchoring. J. Biol. Chem. 285, 32684-32688
    • (2010) J. Biol. Chem , vol.285 , pp. 32684-32688
    • Casteel, D.E.1    Smith-Nguyen, E.V.2    Sankaran, B.3    Roh, S.H.4    Pilz, R.B.5    Kim, C.6
  • 41
    • 0036445512 scopus 로고    scopus 로고
    • Analysis of α-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation
    • Strelkov, S. V., and Burkhard, P. (2002) Analysis of α-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation. J. Struct. Biol. 137, 54-64
    • (2002) J. Struct. Biol , vol.137 , pp. 54-64
    • Strelkov, S.V.1    Burkhard, P.2
  • 42
    • 1642483424 scopus 로고    scopus 로고
    • The structural GDP/GTP cycle of Rab11 reveals a novel interface involved in the dynamics of recycling endosomes
    • Pasqualato, S., Senic-Matuglia, F., Renault, L., Goud, B., Salamero, J., and Cherfils, J. (2004) The structural GDP/GTP cycle of Rab11 reveals a novel interface involved in the dynamics of recycling endosomes. J. Biol. Chem. 279, 11480-11488
    • (2004) J. Biol. Chem , vol.279 , pp. 11480-11488
    • Pasqualato, S.1    Senic-Matuglia, F.2    Renault, L.3    Goud, B.4    Salamero, J.5    Cherfils, J.6
  • 43
    • 0034714574 scopus 로고    scopus 로고
    • Rab11b is essential for recycling of transferrin to the plasma membrane
    • Schlierf, B., Fey, G. H., Hauber, J., Hocke, G. M., and Rosorius, O. (2000) Rab11b is essential for recycling of transferrin to the plasma membrane. Exp. Cell Res. 259, 257-265
    • (2000) Exp. Cell Res , vol.259 , pp. 257-265
    • Schlierf, B.1    Fey, G.H.2    Hauber, J.3    Hocke, G.M.4    Rosorius, O.5
  • 44
    • 24344487878 scopus 로고    scopus 로고
    • Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: Application to cGMP-dependent protein kinase Iα
    • Schnell, J. R., Zhou, G. P., Zweckstetter, M., Rigby, A. C., and Chou, J. J. (2005) Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Iα. Protein Sci. 14, 2421-2428
    • (2005) Protein Sci , vol.14 , pp. 2421-2428
    • Schnell, J.R.1    Zhou, G.P.2    Zweckstetter, M.3    Rigby, A.C.4    Chou, J.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.