메뉴 건너뛰기




Volumn 71, Issue 4, 2008, Pages 1597-1606

Calcineurin B-like domains in the large regulatory α/β subunits of phosphorylase kinase

Author keywords

Calcineurin B like; Calcium; EF hand; Hydrophobic cluster analysis; Phosphorylase kinase; Profile based sequence comparison; Sequence analysis

Indexed keywords

CALCINEURIN; CALCINEURIN B LIKE DOMAIN; PHOSPHORYLASE KINASE;

EID: 44349105965     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22006     Document Type: Article
Times cited : (11)

References (53)
  • 3
    • 0032462546 scopus 로고    scopus 로고
    • Structures of EF-hand Ca(2+)-binding proteins: Diversity in the organization, packing and response to Ca2+ binding
    • Nelson MR, Chazin WJ. Structures of EF-hand Ca(2+)-binding proteins: diversity in the organization, packing and response to Ca2+ binding. Biometals 1998;11:297-318.
    • (1998) Biometals , vol.11 , pp. 297-318
    • Nelson, M.R.1    Chazin, W.J.2
  • 4
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: A prototypical calcium sensor
    • Chin D, Means AR. Calmodulin: a prototypical calcium sensor. Trends Cell Biol 2000;10:322-328.
    • (2000) Trends Cell Biol , vol.10 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 6
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: Diversity in target recognition and activation mechanisms
    • Hoeflich KP, Ikura M. Calmodulin in action: diversity in target recognition and activation mechanisms. Cell 2002;108:739-742.
    • (2002) Cell , vol.108 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 7
    • 33646761687 scopus 로고    scopus 로고
    • Structural basis for diversity of the EF-hand calcium-binding proteins
    • Grabarek Z. Structural basis for diversity of the EF-hand calcium-binding proteins. J Mol Biol 2006;359:509-525.
    • (2006) J Mol Biol , vol.359 , pp. 509-525
    • Grabarek, Z.1
  • 9
    • 0029149085 scopus 로고
    • Molecular and structural basis of target recognition by calmodulin
    • Crivici A, Ikura M. Molecular and structural basis of target recognition by calmodulin. Annu Rev Biophys Biomol Struct 1995;24:85-116.
    • (1995) Annu Rev Biophys Biomol Struct , vol.24 , pp. 85-116
    • Crivici, A.1    Ikura, M.2
  • 10
    • 33751539464 scopus 로고    scopus 로고
    • Protein-protein interactions in the allosteric regulation of protein kinases
    • Pellicena P, Kuriyan J. Protein-protein interactions in the allosteric regulation of protein kinases. Curr Opin Struct Biol 2006;16:702-709.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 702-709
    • Pellicena, P.1    Kuriyan, J.2
  • 11
    • 4744343507 scopus 로고    scopus 로고
    • Regulation of calcium/calmodulin-dependent protein kinase II activation by intramolecular and intermolecular interactions
    • Griffith LC. Regulation of calcium/calmodulin-dependent protein kinase II activation by intramolecular and intermolecular interactions. J Neurosci 2004;24:8394-8398.
    • (2004) J Neurosci , vol.24 , pp. 8394-8398
    • Griffith, L.C.1
  • 13
    • 0034949516 scopus 로고    scopus 로고
    • Molecular characterization of functional domains in the protein kinase SOS2 that is required for plant salt tolerance
    • Guo Y, Halfter U, Ishitani M, Zhu JK. Molecular characterization of functional domains in the protein kinase SOS2 that is required for plant salt tolerance. Plant Cell 2001;13:1383-1400.
    • (2001) Plant Cell , vol.13 , pp. 1383-1400
    • Guo, Y.1    Halfter, U.2    Ishitani, M.3    Zhu, J.K.4
  • 14
    • 1642465539 scopus 로고    scopus 로고
    • The SOS3 family of calcium sensors and SOS2 family of protein kinases in Arabidopsis
    • Gong D, Guo Y, Schumaker KS, Zhu JK. The SOS3 family of calcium sensors and SOS2 family of protein kinases in Arabidopsis. Plant Physiol 2004;134:919-926.
    • (2004) Plant Physiol , vol.134 , pp. 919-926
    • Gong, D.1    Guo, Y.2    Schumaker, K.S.3    Zhu, J.K.4
  • 15
    • 0029020282 scopus 로고
    • Protein kinases 6. The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks SK, Hunter T. Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J 1995;9:576-596.
    • (1995) FASEB J , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 16
    • 0033567657 scopus 로고    scopus 로고
    • Phosphorylase kinase: The complexity of its regulation is reflected in the complexity of its structure
    • Brushia RJ, Walsh DA. Phosphorylase kinase: the complexity of its regulation is reflected in the complexity of its structure. Front Biosci 1999;4:D618-D641.
    • (1999) Front Biosci , vol.4
    • Brushia, R.J.1    Walsh, D.A.2
  • 17
    • 0029145794 scopus 로고
    • Characterization of the regulatory domain of the gamma-subunit of phosphorylase kinase. The two noncontiguous calmodulin-binding subdomains are also autoinhibitory
    • Dasgupta M, Blumenthal DK. Characterization of the regulatory domain of the gamma-subunit of phosphorylase kinase. The two noncontiguous calmodulin-binding subdomains are also autoinhibitory. J Biol Chem 1995;270:22283-22289.
    • (1995) J Biol Chem , vol.270 , pp. 22283-22289
    • Dasgupta, M.1    Blumenthal, D.K.2
  • 18
    • 0024210414 scopus 로고
    • The α and β subunits of phosphorylase kinase are homologous: CDNA cloning and primary structure of the beta subunit
    • Kilimann MW, Zander NF, Kuhn CC, Crabb JW, Meyer HE, Heilmeyer LM, Jr. The α and β subunits of phosphorylase kinase are homologous: cDNA cloning and primary structure of the beta subunit. Proc Natl Acad Sci USA 1988;85:9381-9385.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 9381-9385
    • Kilimann, M.W.1    Zander, N.F.2    Kuhn, C.C.3    Crabb, J.W.4    Meyer, H.E.5    Heilmeyer Jr., L.M.6
  • 19
    • 0020508475 scopus 로고
    • Characterization of initial autophosphorylation events in rabbit skeletal muscle phosphorylase kinase
    • King MM, Fitzgerald TJ, Carlson GM. Characterization of initial autophosphorylation events in rabbit skeletal muscle phosphorylase kinase. J Biol Chem 1983;258:9925-9930.
    • (1983) J Biol Chem , vol.258 , pp. 9925-9930
    • King, M.M.1    Fitzgerald, T.J.2    Carlson, G.M.3
  • 20
    • 0041842499 scopus 로고    scopus 로고
    • Glucoamylase-like domains in the α- and β-subunits of phosphorylase kinase
    • Pallen MJ. Glucoamylase-like domains in the α- and β-subunits of phosphorylase kinase. Protein Sci 2003;12:1804-1807.
    • (2003) Protein Sci , vol.12 , pp. 1804-1807
    • Pallen, M.J.1
  • 22
    • 33846630895 scopus 로고    scopus 로고
    • A generalized analysis of hydrophobic and loop clusters within globular protein sequences
    • Eudes R, Le Tuan K, Delettre J, Mornon JP, Callebaut I. A generalized analysis of hydrophobic and loop clusters within globular protein sequences. BMC Struct Biol 2007;7:2.
    • (2007) BMC Struct Biol , vol.7 , pp. 2
    • Eudes, R.1    Le Tuan, K.2    Delettre, J.3    Mornon, J.P.4    Callebaut, I.5
  • 23
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
    • Gaboriaud C, Bissery V, Benchetrit T, Mornon JP. Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett 1987;224:149-155.
    • (1987) FEBS Lett , vol.224 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4
  • 24
    • 0026475673 scopus 로고
    • Detection of secondary structure elements in proteins by hydrophobic cluster analysis
    • Woodcock S, Mornon JP, Henrissat B. Detection of secondary structure elements in proteins by hydrophobic cluster analysis. Protein Eng 1992;5:629-635.
    • (1992) Protein Eng , vol.5 , pp. 629-635
    • Woodcock, S.1    Mornon, J.P.2    Henrissat, B.3
  • 25
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: Exploring protein sequences for globularity and disorder
    • Linding R, Russell RB, Neduva V, Gibson TJ. GlobPlot: Exploring protein sequences for globularity and disorder. Nucleic Acids Res 2003;31:3701-3708.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 26
    • 34347388470 scopus 로고    scopus 로고
    • UniRef: Comprehensive and non-redundant UniProt reference clusters
    • Suzek BE, Huang H, McGarvey P, Mazumder R, Wu C. UniRef: comprehensive and non-redundant UniProt reference clusters. Bioinformatics 2007;23:1282-1288.
    • (2007) Bioinformatics , vol.23 , pp. 1282-1288
    • Suzek, B.E.1    Huang, H.2    McGarvey, P.3    Mazumder, R.4    Wu, C.5
  • 27
    • 0037100671 scopus 로고    scopus 로고
    • MAFFT: A novel method for rapid multiple sequence alignment based on fast Fourier transform
    • Katoh K, Misawa K, Kuma K, Miyata T. MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform. Nucleic Acids Res 2002;30:3059-3066.
    • (2002) Nucleic Acids Res , vol.30 , pp. 3059-3066
    • Katoh, K.1    Misawa, K.2    Kuma, K.3    Miyata, T.4
  • 29
    • 0032534020 scopus 로고    scopus 로고
    • Populations of hydrophobic amino acids within protein globular domains: Identification of conserved " topohydrophobic" positions
    • Poupon A, Mornon JP. Populations of hydrophobic amino acids within protein globular domains: identification of conserved " topohydrophobic" positions. Proteins 1998;33:329-342.
    • (1998) Proteins , vol.33 , pp. 329-342
    • Poupon, A.1    Mornon, J.P.2
  • 30
    • 0035165967 scopus 로고    scopus 로고
    • A database and tools for 3-D protein structure comparison and alignment using the Combinatorial Extension (CE) algorithm
    • Shindyalov IN, Bourne PE. A database and tools for 3-D protein structure comparison and alignment using the Combinatorial Extension (CE) algorithm. Nucleic Acids Res 2001;29:228-229.
    • (2001) Nucleic Acids Res , vol.29 , pp. 228-229
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 31
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • Soding J. Protein homology detection by HMM-HMM comparison. Bioinformatics 2005;21:951-960.
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Soding, J.1
  • 32
    • 0026100921 scopus 로고
    • A workbench for multiple alignment construction and analysis
    • Schuler GD, Altschul SF, Lipman DJ. A workbench for multiple alignment construction and analysis. Proteins 1991;9:180-190.
    • (1991) Proteins , vol.9 , pp. 180-190
    • Schuler, G.D.1    Altschul, S.F.2    Lipman, D.J.3
  • 33
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley LA, MacCallum RM, Sternberg MJ. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J Mol Biol 2000;299:499-520.
    • (2000) J Mol Biol , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 34
    • 0038634975 scopus 로고    scopus 로고
    • Improvement of the GenTHREADER method for genomic fold recognition
    • McGuffin LJ, Jones DT. Improvement of the GenTHREADER method for genomic fold recognition. Bioinformatics 2003;19:874-881.
    • (2003) Bioinformatics , vol.19 , pp. 874-881
    • McGuffin, L.J.1    Jones, D.T.2
  • 36
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N, Peitsch MC. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997;18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 38
    • 0037305939 scopus 로고    scopus 로고
    • Domains, motifs and clusters in the protein universe
    • Liu J, Rost B. Domains, motifs and clusters in the protein universe. Curr Opin Chem Biol 2003;7:5-11.
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 5-11
    • Liu, J.1    Rost, B.2
  • 39
    • 0142242192 scopus 로고    scopus 로고
    • The crystal structure of the novel calcium-binding protein AtCBL2 from Arabidopsis thaliana
    • Nagae M, Nozawa A, Koizumi N, Sano H, Hashimoto H, Sato M, Shimizu T. The crystal structure of the novel calcium-binding protein AtCBL2 from Arabidopsis thaliana. J Biol Chem 2003;278:42240-42246.
    • (2003) J Biol Chem , vol.278 , pp. 42240-42246
    • Nagae, M.1    Nozawa, A.2    Koizumi, N.3    Sano, H.4    Hashimoto, H.5    Sato, M.6    Shimizu, T.7
  • 40
    • 11844292846 scopus 로고    scopus 로고
    • The structure of the Arabidopsis thaliana SOS3: Molecular mechanism of sensing calcium for salt stress response
    • Sanchez-Barrena MJ, Martinez-Ripoll M, Zhu JK, Albert A. The structure of the Arabidopsis thaliana SOS3: molecular mechanism of sensing calcium for salt stress response. J Mol Biol 2005;345:1253-1264.
    • (2005) J Mol Biol , vol.345 , pp. 1253-1264
    • Sanchez-Barrena, M.J.1    Martinez-Ripoll, M.2    Zhu, J.K.3    Albert, A.4
  • 41
    • 34247627317 scopus 로고    scopus 로고
    • The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3
    • Sanchez-Barrena MJ, Fujii H, Angulo I, Martinez-Ripoll M, Zhu JK, Albert A. The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3. Mol Cell 2007;26:427-435.
    • (2007) Mol Cell , vol.26 , pp. 427-435
    • Sanchez-Barrena, M.J.1    Fujii, H.2    Angulo, I.3    Martinez-Ripoll, M.4    Zhu, J.K.5    Albert, A.6
  • 42
    • 0025129872 scopus 로고
    • Hydrophobic cluster analysis: Procedures to derive structural and functional information from 2-D-representation of protein sequences
    • Lemesle-Varloot L, Henrissat B, Gaboriaud C, Bissery V, Morgat A, Mornon JP. Hydrophobic cluster analysis: procedures to derive structural and functional information from 2-D-representation of protein sequences. Biochimie 1990;72:555-574.
    • (1990) Biochimie , vol.72 , pp. 555-574
    • Lemesle-Varloot, L.1    Henrissat, B.2    Gaboriaud, C.3    Bissery, V.4    Morgat, A.5    Mornon, J.P.6
  • 43
    • 33744516535 scopus 로고    scopus 로고
    • The cytoskeletal organizing protein Cdc42-interacting protein 4 associates with phosphorylase kinase in skeletal muscle
    • Archila S, King MA, Carlson GM, Rice NA. The cytoskeletal organizing protein Cdc42-interacting protein 4 associates with phosphorylase kinase in skeletal muscle. Biochem Biophys Res Commun 2006;345:1592-1599.
    • (2006) Biochem Biophys Res Commun , vol.345 , pp. 1592-1599
    • Archila, S.1    King, M.A.2    Carlson, G.M.3    Rice, N.A.4
  • 45
    • 0024341971 scopus 로고
    • The γ-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin
    • Dasgupta M, Honeycutt T, Blumenthal DK. The γ-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin. J Biol Chem 1989;264:17156-17163.
    • (1989) J Biol Chem , vol.264 , pp. 17156-17163
    • Dasgupta, M.1    Honeycutt, T.2    Blumenthal, D.K.3
  • 46
    • 0028946237 scopus 로고
    • Identification of the substrate and pseudosubstrate binding sites of phosphorylase kinase gamma-subunit
    • Huang CY, Yuan CJ, Blumenthal DK, Graves DJ. Identification of the substrate and pseudosubstrate binding sites of phosphorylase kinase gamma-subunit. J Biol Chem 1995;270:7183-7188.
    • (1995) J Biol Chem , vol.270 , pp. 7183-7188
    • Huang, C.Y.1    Yuan, C.J.2    Blumenthal, D.K.3    Graves, D.J.4
  • 47
    • 15944365450 scopus 로고    scopus 로고
    • 2+/CaM in complex with the phosphorylase kinase PhK5 peptide
    • 2+/CaM in complex with the phosphorylase kinase PhK5 peptide. FEBS J 2005;272:1511-1522.
    • (2005) FEBS J , vol.272 , pp. 1511-1522
    • Cook, A.G.1    Johnson, L.N.2    McDonnell, J.M.3
  • 48
    • 0023655530 scopus 로고
    • Characterization of the calmodulin-binding sites of muscle phosphofructokinase and comparison with known calmodulin-binding domains
    • Buschmeier B, Meyer HE, Mayr GW. Characterization of the calmodulin-binding sites of muscle phosphofructokinase and comparison with known calmodulin-binding domains. J Biol Chem 1987; 262:9454-9462.
    • (1987) J Biol Chem , vol.262 , pp. 9454-9462
    • Buschmeier, B.1    Meyer, H.E.2    Mayr, G.W.3
  • 50
    • 0022972435 scopus 로고
    • The refined structure of vitamin D-dependent calcium-binding protein from bovine intestine. Molecular details, ion binding, and implications for the structure of other calcium-binding proteins
    • Szebenyi DM, Moffat K. The refined structure of vitamin D-dependent calcium-binding protein from bovine intestine. Molecular details, ion binding, and implications for the structure of other calcium-binding proteins. J Biol Chem 1986;261:8761-8777.
    • (1986) J Biol Chem , vol.261 , pp. 8761-8777
    • Szebenyi, D.M.1    Moffat, K.2
  • 51
    • 0034730245 scopus 로고    scopus 로고
    • 2+/Calmodulin-dependent protein kinase. Role of the neural visinin-like domain in regulating autophosphorylation and calmodulin affinity
    • 2+/Calmodulin-dependent protein kinase. Role of the neural visinin-like domain in regulating autophosphorylation and calmodulin affinity. J Biol Chem 2000;275:30417-30422.
    • (2000) J Biol Chem , vol.275 , pp. 30417-30422
    • Sathyanarayanan, P.V.1    Cremo, C.R.2    Poovaiah, B.W.3
  • 52
    • 0020490661 scopus 로고
    • Rabbit skeletal muscle phosphorylase kinase. Catalytic and regulatory properties of the active alpha gamma delta and gamma delta complexes
    • Chan KF, Graves DJ. Rabbit skeletal muscle phosphorylase kinase. Catalytic and regulatory properties of the active alpha gamma delta and gamma delta complexes. J Biol Chem 1982;257:5948-5955.
    • (1982) J Biol Chem , vol.257 , pp. 5948-5955
    • Chan, K.F.1    Graves, D.J.2
  • 53
    • 0036155785 scopus 로고    scopus 로고
    • Three-dimensional structure of phosphorylase kinase at 22 A resolution and its complex with glycogen phosphorylase b
    • Venien-Bryan C, Lowe EM, Boisset N, Traxler KW, Johnson LN, Carlson GM. Three-dimensional structure of phosphorylase kinase at 22 A resolution and its complex with glycogen phosphorylase b. Structure 2002;10:33-41.
    • (2002) Structure , vol.10 , pp. 33-41
    • Venien-Bryan, C.1    Lowe, E.M.2    Boisset, N.3    Traxler, K.W.4    Johnson, L.N.5    Carlson, G.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.