메뉴 건너뛰기




Volumn 63, Issue 4, 2006, Pages 727-732

Conformational flexibility may explain multiple cellular roles of PEST motifs

Author keywords

[No Author keywords available]

Indexed keywords

CALPAIN; CASPASE; PROTEIN; UBIQUITIN;

EID: 33646767065     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.20918     Document Type: Article
Times cited : (17)

References (49)
  • 1
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers S, Wells R, Rechsteiner M. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 1986; 234:364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 2
    • 2542470460 scopus 로고    scopus 로고
    • Slac2-a/melanophilin contains multiple PEST-like sequences that are highly sensitive to proteolysis
    • Fukuda M, Itoh T. Slac2-a/melanophilin contains multiple PEST-like sequences that are highly sensitive to proteolysis. J Biol Chem 2004;279:22314-22321.
    • (2004) J Biol Chem , vol.279 , pp. 22314-22321
    • Fukuda, M.1    Itoh, T.2
  • 3
    • 0141844589 scopus 로고    scopus 로고
    • Phosphorylation of a pest sequence in ABCA1 promotes calpain degradation and is reversed by ApoA-I
    • Martinez LO, Agerholm-Larsen B, Wang N, Chen W, Tall AR. Phosphorylation of a pest sequence in ABCA1 promotes calpain degradation and is reversed by ApoA-I. J Biol Chem 2003;278: 37368-37374.
    • (2003) J Biol Chem , vol.278 , pp. 37368-37374
    • Martinez, L.O.1    Agerholm-Larsen, B.2    Wang, N.3    Chen, W.4    Tall, A.R.5
  • 4
    • 4544345125 scopus 로고    scopus 로고
    • Caspase-mediated specific cleavage of human histone deacetylase 4
    • Liu F, Dowling M, Yang XJ, Kao GD. Caspase-mediated specific cleavage of human histone deacetylase 4. J Biol Chem 2004;279: 34537-34546.
    • (2004) J Biol Chem , vol.279 , pp. 34537-34546
    • Liu, F.1    Dowling, M.2    Yang, X.J.3    Kao, G.D.4
  • 5
    • 0033595636 scopus 로고    scopus 로고
    • The PEST domain of IkappaBalpha is necessary and sufficient for in vitro degradation by mu-calpain
    • Shumway SD, Maki M, Miyamoto S. The PEST domain of IkappaBalpha is necessary and sufficient for in vitro degradation by mu-calpain. J Biol Chem 1999;274:30874-30881.
    • (1999) J Biol Chem , vol.274 , pp. 30874-30881
    • Shumway, S.D.1    Maki, M.2    Miyamoto, S.3
  • 6
    • 0036272369 scopus 로고    scopus 로고
    • Transferable domain in the G(1) cyclin Cln2 sufficient to switch degradation of Sic1 from the E3 ubiquitin ligase SCF(Cdc4) to SCF(Grr1)
    • Berset C, Griac P, Tempel R, La Rue J, Wittenberg C, Lanker S. Transferable domain in the G(1) cyclin Cln2 sufficient to switch degradation of Sic1 from the E3 ubiquitin ligase SCF(Cdc4) to SCF(Grr1). Mol Cell Biol 2002;22:4463-4476.
    • (2002) Mol Cell Biol , vol.22 , pp. 4463-4476
    • Berset, C.1    Griac, P.2    Tempel, R.3    La Rue, J.4    Wittenberg, C.5    Lanker, S.6
  • 8
    • 0030850174 scopus 로고    scopus 로고
    • Stress and developmental regulation of the yeast C-type cyclin Ume3p (Srb11p/Ssn8p)
    • Cooper KF, Mallory MJ, Smith JB, Strich R. Stress and developmental regulation of the yeast C-type cyclin Ume3p (Srb11p/Ssn8p). EMBO J 1997;16:4665-4675.
    • (1997) EMBO J , vol.16 , pp. 4665-4675
    • Cooper, K.F.1    Mallory, M.J.2    Smith, J.B.3    Strich, R.4
  • 9
    • 0037200042 scopus 로고    scopus 로고
    • Identification and characterization of HIPK2 interacting with p73 and modulating functions of the p53 family in vivo
    • Kim EJ, Park JS, Um SJ. Identification and characterization of HIPK2 interacting with p73 and modulating functions of the p53 family in vivo. J Biol Chem 2002;277:32020-32028.
    • (2002) J Biol Chem , vol.277 , pp. 32020-32028
    • Kim, E.J.1    Park, J.S.2    Um, S.J.3
  • 10
    • 1542317686 scopus 로고    scopus 로고
    • US11 of herpes simplex virus type 1 interacts with HIPK2 and antagonizes HIPK2-induced cell growth arrest
    • Giraud S, Diaz-Latoud C, Hacot S, Textoris J, Bourette RP, Diaz JJ. US11 of herpes simplex virus type 1 interacts with HIPK2 and antagonizes HIPK2-induced cell growth arrest. J Virol 2004;78: 2984-2993.
    • (2004) J Virol , vol.78 , pp. 2984-2993
    • Giraud, S.1    Diaz-Latoud, C.2    Hacot, S.3    Textoris, J.4    Bourette, R.P.5    Diaz, J.J.6
  • 11
    • 0029851617 scopus 로고    scopus 로고
    • Signal-induced degradation of I(kappa)B(alpha): Association with NF-kappaB and the PEST sequence in I(kappa)B(alpha) are not required
    • Van Antwerp DJ, Verma IM. Signal-induced degradation of I(kappa)B(alpha): association with NF-kappaB and the PEST sequence in I(kappa)B(alpha) are not required. Mol Cell Biol 1996;16:6037-6045.
    • (1996) Mol Cell Biol , vol.16 , pp. 6037-6045
    • Van Antwerp, D.J.1    Verma, I.M.2
  • 14
    • 0035853847 scopus 로고    scopus 로고
    • The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover
    • Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. J Biol Chem 2001;276:12301-12309.
    • (2001) J Biol Chem , vol.276 , pp. 12301-12309
    • Huber, A.H.1    Stewart, D.B.2    Laurents, D.V.3    Nelson, W.J.4    Weis, W.I.5
  • 15
    • 30144437939 scopus 로고    scopus 로고
    • Intrinsic unstructuredness and abundance of PEST motifs in eukaryotic proteomes
    • Singh GP, Ganapathi M, Sandhu KS, Dash D. Intrinsic unstructuredness and abundance of PEST motifs in eukaryotic proteomes. Proteins 2005;62:309-315.
    • (2005) Proteins , vol.62 , pp. 309-315
    • Singh, G.P.1    Ganapathi, M.2    Sandhu, K.S.3    Dash, D.4
  • 16
    • 0027981730 scopus 로고
    • The conformational analysis of a synthetic S4 peptide corresponding to a voltage-gated potassium ion channel protein
    • Haris PI, Ramesh B, Brazier S, Chapman D. The conformational analysis of a synthetic S4 peptide corresponding to a voltage-gated potassium ion channel protein. FEBS Lett 1994;349:371-374.
    • (1994) FEBS Lett , vol.349 , pp. 371-374
    • Haris, P.I.1    Ramesh, B.2    Brazier, S.3    Chapman, D.4
  • 17
    • 12144275312 scopus 로고    scopus 로고
    • Structural flexibility of small GTPases. Can it explain their functional versatility?
    • Helmreich EJ. Structural flexibility of small GTPases. Can it explain their functional versatility? Biol Chem 2004;385:1121-1136.
    • (2004) Biol Chem , vol.385 , pp. 1121-1136
    • Helmreich, E.J.1
  • 18
    • 2442645033 scopus 로고    scopus 로고
    • Proteasomes begin ornithine decarboxylase digestion at the C terminus
    • Zhang M, MacDonald AI, Hoyt MA, Coffino P. Proteasomes begin ornithine decarboxylase digestion at the C terminus. J Biol Chem 2004;279:20959-20965.
    • (2004) J Biol Chem , vol.279 , pp. 20959-20965
    • Zhang, M.1    MacDonald, A.I.2    Hoyt, M.A.3    Coffino, P.4
  • 19
    • 0023140225 scopus 로고
    • Correlation among sites of limited proteolysis, enzyme accessibility and segmental mobility
    • Novotny J, Bruccoleri RE. Correlation among sites of limited proteolysis, enzyme accessibility and segmental mobility. FEBS Lett 1987;211:185-189.
    • (1987) FEBS Lett , vol.211 , pp. 185-189
    • Novotny, J.1    Bruccoleri, R.E.2
  • 20
    • 0023055086 scopus 로고
    • Correlation between sites of limited proteolysis and segmental mobility in thermolysin
    • Fontana A, Fassina G, Vita C, Dalzoppo D, Zamai M, and Zambonin M. Correlation between sites of limited proteolysis and segmental mobility in thermolysin. Biochemistry 1986;25:1847-1851.
    • (1986) Biochemistry , vol.25 , pp. 1847-1851
    • Fontana, A.1    Fassina, G.2    Vita, C.3    Dalzoppo, D.4    Zamai, M.5    Zambonin, M.6
  • 21
    • 2442672732 scopus 로고    scopus 로고
    • Modulation of the structural integrity of helix F in apomyoglobin by single amino acid replacements
    • Picotti P, Marabotti A, Negro A, Musi V, Spolaore B, Zambonin M, Fontana A. Modulation of the structural integrity of helix F in apomyoglobin by single amino acid replacements. Protein Sci 2004;13:1572-1585.
    • (2004) Protein Sci , vol.13 , pp. 1572-1585
    • Picotti, P.1    Marabotti, A.2    Negro, A.3    Musi, V.4    Spolaore, B.5    Zambonin, M.6    Fontana, A.7
  • 22
    • 0022555901 scopus 로고
    • Study of protein dynamics by X-ray diffraction
    • Ringe D, Petsko GA. Study of protein dynamics by X-ray diffraction. Methods Enzymol 1986;131:389-433.
    • (1986) Methods Enzymol , vol.131 , pp. 389-433
    • Ringe, D.1    Petsko, G.A.2
  • 23
    • 0033955909 scopus 로고    scopus 로고
    • Protein thermal stability: Insights from atomic displacement parameters (B values)
    • Parthasarathy S, Murthy MR. Protein thermal stability: insights from atomic displacement parameters (B values). Protein Eng 2000;13:9-13.
    • (2000) Protein Eng , vol.13 , pp. 9-13
    • Parthasarathy, S.1    Murthy, M.R.2
  • 24
    • 0037316987 scopus 로고    scopus 로고
    • Flexibility analysis of enzyme active sites by crystallographic temperature factors
    • Yuan Z, Zhao J, Wang ZX. Flexibility analysis of enzyme active sites by crystallographic temperature factors. Protein Eng 2003;16: 109-114.
    • (2003) Protein Eng , vol.16 , pp. 109-114
    • Yuan, Z.1    Zhao, J.2    Wang, Z.X.3
  • 26
    • 0027092679 scopus 로고
    • The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X-ray structures
    • Hyberts SG, Goldberg MS, Havel TF, Wagner G. The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X-ray structures. Protein Sci 1992;1:736-751.
    • (1992) Protein Sci , vol.1 , pp. 736-751
    • Hyberts, S.G.1    Goldberg, M.S.2    Havel, T.F.3    Wagner, G.4
  • 27
    • 0037250308 scopus 로고    scopus 로고
    • PDB-REPRDB: A database of representa-tive protein chains from the Protein Data Bank (PDB) in 2003
    • Noguchi T, Akiyama Y. PDB-REPRDB: a database of representa-tive protein chains from the Protein Data Bank (PDB) in 2003. Nucleic Acids Res 2003;31:492-493.
    • (2003) Nucleic Acids Res , vol.31 , pp. 492-493
    • Noguchi, T.1    Akiyama, Y.2
  • 28
    • 0028109886 scopus 로고
    • Conservation and prediction of solvent accessibility in protein families
    • Rost B, Sander C. Conservation and prediction of solvent accessibility in protein families. Proteins 1994;20:216-226.
    • (1994) Proteins , vol.20 , pp. 216-226
    • Rost, B.1    Sander, C.2
  • 30
    • 12544252739 scopus 로고    scopus 로고
    • The key role of protein flexibility in modulating IgE interactions
    • Price NE, Price NC, Kelly SM, McDonnell JM. The key role of protein flexibility in modulating IgE interactions. J Biol Chem 2005;280:2324-2330.
    • (2005) J Biol Chem , vol.280 , pp. 2324-2330
    • Price, N.E.1    Price, N.C.2    Kelly, S.M.3    McDonnell, J.M.4
  • 32
    • 0347994107 scopus 로고    scopus 로고
    • A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function
    • Quigley PM, Korotkov K, Baneyx F, Hol WG. A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function. Protein Sci 2004;13:269-277.
    • (2004) Protein Sci , vol.13 , pp. 269-277
    • Quigley, P.M.1    Korotkov, K.2    Baneyx, F.3    Hol, W.G.4
  • 33
    • 0030018850 scopus 로고    scopus 로고
    • Structural flexibility modulates the activity of human glutathione transferase P1-1. Role of helix 2 flexibility in the catalytic mechanism
    • Ricci G, Caccuri AM, Lo Bello M, Rosato N, Mei G, Nicotra M, Chiessi E, Mazzetti AP, Federici G. Structural flexibility modulates the activity of human glutathione transferase P1-1. Role of helix 2 flexibility in the catalytic mechanism. J Biol Chem 1996;271:16187-16192.
    • (1996) J Biol Chem , vol.271 , pp. 16187-16192
    • Ricci, G.1    Caccuri, A.M.2    Lo Bello, M.3    Rosato, N.4    Mei, G.5    Nicotra, M.6    Chiessi, E.7    Mazzetti, A.P.8    Federici, G.9
  • 34
    • 0842324785 scopus 로고    scopus 로고
    • The nucleosome: From genomic organization to genomic regulation
    • Khorasanizadeh S. The nucleosome: from genomic organization to genomic regulation. Cell 2004;116:259-272.
    • (2004) Cell , vol.116 , pp. 259-272
    • Khorasanizadeh, S.1
  • 35
    • 0033529565 scopus 로고    scopus 로고
    • Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome
    • Kornberg RD, Lorch Y. Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome. Cell 1999;98: 285-294.
    • (1999) Cell , vol.98 , pp. 285-294
    • Kornberg, R.D.1    Lorch, Y.2
  • 37
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, Wright PE. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 2005;6:197-208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 38
    • 0031030057 scopus 로고    scopus 로고
    • Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum
    • Akopian TN, Kisselev AF, Goldberg AL. Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum. J Biol Chem 1997;272:1791-1798.
    • (1997) J Biol Chem , vol.272 , pp. 1791-1798
    • Akopian, T.N.1    Kisselev, A.F.2    Goldberg, A.L.3
  • 39
    • 0018496246 scopus 로고
    • Reconstitution of aminotransferases in vivo and their metabolic turnover
    • Perry ST, Lee KL, Kenney FT. Reconstitution of aminotransferases in vivo and their metabolic turnover. Arch Biochem Biophys 1979;195:362-367.
    • (1979) Arch Biochem Biophys , vol.195 , pp. 362-367
    • Perry, S.T.1    Lee, K.L.2    Kenney, F.T.3
  • 40
    • 0028951190 scopus 로고
    • Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway
    • Johnston JA, Johnson ES, Waller PR, Varshavsky A. Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway. J Biol Chem 1995;270:8172-8178.
    • (1995) J Biol Chem , vol.270 , pp. 8172-8178
    • Johnston, J.A.1    Johnson, E.S.2    Waller, P.R.3    Varshavsky, A.4
  • 41
    • 0042329502 scopus 로고    scopus 로고
    • Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine
    • Kenniston JA, Baker TA, Fernandez JM, Sauer RT. Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine. Cell 2003;114:511-520.
    • (2003) Cell , vol.114 , pp. 511-520
    • Kenniston, J.A.1    Baker, T.A.2    Fernandez, J.M.3    Sauer, R.T.4
  • 42
    • 4344559454 scopus 로고    scopus 로고
    • An unstructured initiation site is required for efficient proteasome-mediated degradation
    • Prakash S, Tian L, Ratliff KS, Lehotzky RE, Matouschek A. An unstructured initiation site is required for efficient proteasome-mediated degradation. Nat Struct Mol Biol 2004;11:830-837.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 830-837
    • Prakash, S.1    Tian, L.2    Ratliff, K.S.3    Lehotzky, R.E.4    Matouschek, A.5
  • 43
    • 4344691452 scopus 로고    scopus 로고
    • NPDC-1, a novel regulator of neuronal proliferation, is degraded by the ubiquitin/proteasome system through a PEST degradation motif
    • Spencer ML, Theodosiou M, Noonan DJ. NPDC-1, a novel regulator of neuronal proliferation, is degraded by the ubiquitin/proteasome system through a PEST degradation motif. J Biol Chem 2004;279:37069-37078.
    • (2004) J Biol Chem , vol.279 , pp. 37069-37078
    • Spencer, M.L.1    Theodosiou, M.2    Noonan, D.J.3
  • 44
    • 0031439931 scopus 로고    scopus 로고
    • A role for CKII phosphorylation of the cactus PEST domain in dorsoventral patterning of the Drosophila embryo
    • Liu ZP, Galindo RL, Wasserman SA. A role for CKII phosphorylation of the cactus PEST domain in dorsoventral patterning of the Drosophila embryo. Genes Dev 1997;11:3413-3422.
    • (1997) Genes Dev , vol.11 , pp. 3413-3422
    • Liu, Z.P.1    Galindo, R.L.2    Wasserman, S.A.3
  • 45
    • 0029670085 scopus 로고    scopus 로고
    • Phosphorylation of IkappaBalpha in the C-terminal PEST domain by casein kinase II affects intrinsic protein stability
    • Lin R, Beauparlant P, Makris C, Meloche S, Hiscott J. Phosphorylation of IkappaBalpha in the C-terminal PEST domain by casein kinase II affects intrinsic protein stability. Mol Cell Biol 1996;16: 1401-1409.
    • (1996) Mol Cell Biol , vol.16 , pp. 1401-1409
    • Lin, R.1    Beauparlant, P.2    Makris, C.3    Meloche, S.4    Hiscott, J.5
  • 46
    • 0030833432 scopus 로고    scopus 로고
    • O-Glycosylation of C-terminal tandem-repeated sequences regulates the secretion of rat pancreatic bile salt-dependent lipase
    • Bruneau N, Nganga A, Fisher EA, Lombardo D. O-Glycosylation of C-terminal tandem-repeated sequences regulates the secretion of rat pancreatic bile salt-dependent lipase. J Biol Chem 1997;272: 27353-27361.
    • (1997) J Biol Chem , vol.272 , pp. 27353-27361
    • Bruneau, N.1    Nganga, A.2    Fisher, E.A.3    Lombardo, D.4
  • 47
    • 0037088588 scopus 로고    scopus 로고
    • Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity
    • Bies J, Markus J, Wolff L. Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity. J Biol Chem 2002;277:8999-9009.
    • (2002) J Biol Chem , vol.277 , pp. 8999-9009
    • Bies, J.1    Markus, J.2    Wolff, L.3
  • 48
    • 17444411515 scopus 로고    scopus 로고
    • The telomere-binding protein Taz1p as a target for modification by a SUMO-1 homologue in fission yeast
    • Spink K, Ho JC, Tanaka K, Watts FZ, Chambers A. The telomere-binding protein Taz1p as a target for modification by a SUMO-1 homologue in fission yeast. Biochem Genet 2005;43:103-117.
    • (2005) Biochem Genet , vol.43 , pp. 103-117
    • Spink, K.1    Ho, J.C.2    Tanaka, K.3    Watts, F.Z.4    Chambers, A.5
  • 49
    • 0034833014 scopus 로고    scopus 로고
    • Phosphorylation of serine residues affects the conformation of the calmodulin binding domain of human protein 4.1
    • Vetter SW, Leclerc E. Phosphorylation of serine residues affects the conformation of the calmodulin binding domain of human protein 4.1. Eur J Biochem 2001;268:4292-4299.
    • (2001) Eur J Biochem , vol.268 , pp. 4292-4299
    • Vetter, S.W.1    Leclerc, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.