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Volumn 40, Issue 5, 2012, Pages 969-974

Regulation of protein phosphatase 1 by intrinsically disordered proteins

Author keywords

Intrinsically disordered protein; Nuclear magnetic resonance (NMR); Protein phosphatase 1 (PP1); Small angle X ray scattering (SAXS)

Indexed keywords

I 2 PROTEIN; INTRINSICALLY DISORDERED PROTEIN; MYPT1 PROTEIN; PHOSPHOPROTEIN PHOSPHATASE 1; PROTEIN; SPINOPHILIN; UNCLASSIFIED DRUG;

EID: 84866679293     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20120094     Document Type: Review
Times cited : (39)

References (47)
  • 1
    • 61649127812 scopus 로고    scopus 로고
    • From promiscuity to precision: Protein phosphatases get a makeover
    • Virshup, D.M. and Shenolikar, S. (2009) From promiscuity to precision: protein phosphatases get a makeover. Mol. Cell 33, 537-545
    • (2009) Mol. Cell , vol.33 , pp. 537-545
    • Virshup, D.M.1    Shenolikar, S.2
  • 2
    • 70350340056 scopus 로고    scopus 로고
    • Serine/threonine phosphatases: Mechanism through structure
    • Shi, Y. (2009) Serine/threonine phosphatases: mechanism through structure. Cell 139, 468-484
    • (2009) Cell , vol.139 , pp. 468-484
    • Shi, Y.1
  • 3
    • 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. Signaling 2, re9
    • (2009) Sci. Signaling , vol.2
    • Roy, J.1    Cyert, M.S.2
  • 4
    • 84872773091 scopus 로고    scopus 로고
    • Structural basis for protein phosphatase 1 regulation and specificity
    • doi:10.1111/j.1742-4658.2012.08509.x
    • Peti, W., Nairn, A.C. and Page, R. (2012) Structural basis for protein phosphatase 1 regulation and specificity. FEBS J., doi:10.1111/j.1742-4658.2012. 08509.x
    • (2012) FEBS J.
    • Peti, W.1    Nairn, A.C.2    Page, R.3
  • 5
    • 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
  • 8
    • 0027233603 scopus 로고
    • Inhibitor-2 functions like a chaperone to fold three expressed isoforms of mammalian protein phosphatase-1 into a conformation with the specificity and regulatory properties of the native enzyme
    • Alessi, D.R., Street, A.J., Cohen, P. and Cohen, P.T. (1993) Inhibitor-2 functions like a chaperone to fold three expressed isoforms of mammalian protein phosphatase-1 into a conformation with the specificity and regulatory properties of the native enzyme. Eur. J. Biochem. 213, 1055-1066
    • (1993) Eur. J. Biochem. , vol.213 , pp. 1055-1066
    • Alessi, D.R.1    Street, A.J.2    Cohen, P.3    Cohen, P.T.4
  • 9
    • 0033166545 scopus 로고    scopus 로고
    • Beyond the dopamine receptor: The DARPP-32/protein phosphatase-1 cascade
    • Greengard, P., Allen, P.B. and Nairn, A.C. (1999) Beyond the dopamine receptor: the DARPP-32/protein phosphatase-1 cascade. Neuron 23, 435-447
    • (1999) Neuron , vol.23 , pp. 435-447
    • Greengard, P.1    Allen, P.B.2    Nairn, A.C.3
  • 10
    • 0030972388 scopus 로고    scopus 로고
    • Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins
    • Kwon, Y.G., Huang, H.B., Desdouits, F., Girault, J.A., Greengard, P. and Nairn, A.C. (1997) Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins. Proc. Natl. Acad. Sci. U.S.A. 94, 3536-3541
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 3536-3541
    • Kwon, Y.G.1    Huang, H.B.2    Desdouits, F.3    Girault, J.A.4    Greengard, P.5    Nairn, A.C.6
  • 11
    • 0021326226 scopus 로고
    • DARPP-32, a dopamine- and adenosine 3′:5′-monophosphate- regulated phosphoprotein enriched in dopamine-innervated brain regions. II. Purification and characterization of the phosphoprotein from bovine caudate nucleus
    • Hemmings, Jr, H.C., Nairn, A.C., Aswad, D.W. and Greengard, P. (1984) DARPP-32, a dopamine- and adenosine 3′:5′-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. II. Purification and characterization of the phosphoprotein from bovine caudate nucleus. J. Neurosci. 4, 99-110
    • (1984) J. Neurosci. , vol.4 , pp. 99-110
    • Hemmings Jr., H.C.1    Nairn, A.C.2    Aswad, D.W.3    Greengard, P.4
  • 12
    • 0038819929 scopus 로고    scopus 로고
    • Degeneracy and function of the ubiquitous RVXF motif that mediates binding to protein phosphatase-1
    • Wakula, P., Beullens, M., Ceulemans, H., Stalmans, W. and Bollen, M. (2003) Degeneracy and function of the ubiquitous RVXF motif that mediates binding to protein phosphatase-1. J. Biol. Chem. 278, 18817-18823
    • (2003) J. Biol. Chem. , vol.278 , pp. 18817-18823
    • Wakula, P.1    Beullens, M.2    Ceulemans, H.3    Stalmans, W.4    Bollen, M.5
  • 13
    • 30744432348 scopus 로고    scopus 로고
    • Structural analysis of the protein phosphatase 1 docking motif: Molecular description of binding specificities identifies interacting proteins
    • Meiselbach, H., Sticht, H. and Enz, R. (2006) Structural analysis of the protein phosphatase 1 docking motif: molecular description of binding specificities identifies interacting proteins. Chem. Biol. 13, 49-59
    • (2006) Chem. Biol. , vol.13 , pp. 49-59
    • Meiselbach, H.1    Sticht, H.2    Enz, R.3
  • 15
    • 33747768414 scopus 로고    scopus 로고
    • Characterizing residual structure in disordered protein states using nuclear magnetic resonance
    • Eliezer, D. (2007) Characterizing residual structure in disordered protein states using nuclear magnetic resonance. Methods Mol. Biol. 350, 49-67
    • (2007) Methods Mol. Biol. , vol.350 , pp. 49-67
    • Eliezer, D.1
  • 17
    • 79951659237 scopus 로고    scopus 로고
    • Molecular investigations of the structure and function of the protein phosphatase 1-spinophilin-inhibitor 2 heterotrimeric complex
    • Dancheck, B., Ragusa, M.J., Allaire, M., Nairn, A.C., Page, R. and Peti, W. (2011) Molecular investigations of the structure and function of the protein phosphatase 1-spinophilin-inhibitor 2 heterotrimeric complex. Biochemistry 50, 1238-1246
    • (2011) Biochemistry , vol.50 , pp. 1238-1246
    • Dancheck, B.1    Ragusa, M.J.2    Allaire, M.3    Nairn, A.C.4    Page, R.5    Peti, W.6
  • 18
    • 60349087841 scopus 로고    scopus 로고
    • Biophysical characterization of intrinsically disordered proteins
    • Eliezer, D. (2009) Biophysical characterization of intrinsically disordered proteins. Curr. Opin. Struct. Biol. 19, 23-30
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 23-30
    • Eliezer, D.1
  • 19
    • 77956332835 scopus 로고    scopus 로고
    • Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators
    • Marsh, J.A., Dancheck, B., Ragusa, M.J., Allaire, M., Forman-Kay, J.D. and Peti, W. (2010) Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators. Structure 18, 1094-1103
    • (2010) Structure , vol.18 , pp. 1094-1103
    • Marsh, J.A.1    Dancheck, B.2    Ragusa, M.J.3    Allaire, M.4    Forman-Kay, J.D.5    Peti, W.6
  • 21
    • 28044458515 scopus 로고    scopus 로고
    • A structural model for unfolded proteins from residual dipolar couplings and small-angle X-ray scattering
    • Bernado, P., Blanchard, L., Timmins, P., Marion, D., Ruigrok, R.W. and Blackledge, M. (2005) A structural model for unfolded proteins from residual dipolar couplings and small-angle X-ray scattering. Proc. Natl. Acad. Sci. U.S.A. 102, 17002-17007
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 17002-17007
    • Bernado, P.1    Blanchard, L.2    Timmins, P.3    Marion, D.4    Ruigrok, R.W.5    Blackledge, M.6
  • 22
    • 69849103777 scopus 로고    scopus 로고
    • Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings
    • Jensen, M.R., Markwick, P.R., Meier, S., Griesinger, C., Zweckstetter, M., Grzesiek, S., Bernado, P. and Blackledge, M. (2009) Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings. Structure 17, 1169-1185
    • (2009) Structure , vol.17 , pp. 1169-1185
    • Jensen, M.R.1    Markwick, P.R.2    Meier, S.3    Griesinger, C.4    Zweckstetter, M.5    Grzesiek, S.6    Bernado, P.7    Blackledge, M.8
  • 23
    • 77950403640 scopus 로고    scopus 로고
    • Defining conformational ensembles of intrinsically disordered and partially folded proteins directly from chemical shifts
    • Jensen, M.R., Salmon, L., Nodet, G. and Blackledge, M. (2010) Defining conformational ensembles of intrinsically disordered and partially folded proteins directly from chemical shifts. J. Am. Chem. Soc. 132, 1270-1272
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 1270-1272
    • Jensen, M.R.1    Salmon, L.2    Nodet, G.3    Blackledge, M.4
  • 24
    • 0035906650 scopus 로고    scopus 로고
    • Calculation of ensembles of structures representing the unfolded state of an SH3 domain
    • Choy, W.Y. and Forman-Kay, J.D. (2001) Calculation of ensembles of structures representing the unfolded state of an SH3 domain. J. Mol. Biol. 308, 1011-1032
    • (2001) J. Mol. Biol. , vol.308 , pp. 1011-1032
    • Choy, W.Y.1    Forman-Kay, J.D.2
  • 26
    • 67650684936 scopus 로고    scopus 로고
    • Structure and disorder in an unfolded state under nondenaturing conditions from ensemble models consistent with a large number of experimental restraints
    • Marsh, J.A. and Forman-Kay, J.D. (2009) Structure and disorder in an unfolded state under nondenaturing conditions from ensemble models consistent with a large number of experimental restraints. J. Mol. Biol. 391, 359-374
    • (2009) J. Mol. Biol. , vol.391 , pp. 359-374
    • Marsh, J.A.1    Forman-Kay, J.D.2
  • 27
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright, P.E. and Dyson, H.J. (1999) Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293, 321-331
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 29
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: The fly-casting mechanism
    • Shoemaker, B.A., Portman, J.J. and Wolynes, P.G. (2000) Speeding molecular recognition by using the folding funnel: the fly-casting mechanism. Proc. Natl. Acad. Sci. U.S.A. 97, 8868-8873
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 30
    • 14844361449 scopus 로고    scopus 로고
    • Primary contact sites in intrinsically unstructured proteins: The case of calpastatin and microtubule-associated protein 2
    • Csizmok, V., Bokor, M., Banki, P., Klement, E., Medzihradszky, K.F., Friedrich, P., Tompa, K. and Tompa, P. (2005) Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2. Biochemistry 44, 3955-3964
    • (2005) Biochemistry , vol.44 , pp. 3955-3964
    • Csizmok, V.1    Bokor, M.2    Banki, P.3    Klement, E.4    Medzihradszky, K.F.5    Friedrich, P.6    Tompa, K.7    Tompa, P.8
  • 31
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa, P. (2005) The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett. 579, 3346-3354
    • (2005) FEBS Lett. , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 34
    • 77950519767 scopus 로고    scopus 로고
    • Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites
    • Ragusa, M.J., Dancheck, B., Critton, D.A., Nairn, A.C., Page, R. and Peti, W. (2010) Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites. Nat. Struct. Mol. Biol. 17, 459-464
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 459-464
    • Ragusa, M.J.1    Dancheck, B.2    Critton, D.A.3    Nairn, A.C.4    Page, R.5    Peti, W.6
  • 36
    • 3042547846 scopus 로고    scopus 로고
    • Structural basis of protein phosphatase 1 regulation
    • Terrak, M., Kerff, F., Langsetmo, K., Tao, T. and Dominguez, R. (2004) Structural basis of protein phosphatase 1 regulation. Nature 429, 780-784
    • (2004) Nature , vol.429 , pp. 780-784
    • Terrak, M.1    Kerff, F.2    Langsetmo, K.3    Tao, T.4    Dominguez, R.5
  • 38
    • 56749172641 scopus 로고    scopus 로고
    • Detailed structural characterization of unbound protein phosphatase 1 inhibitors
    • Dancheck, B., Nairn, A.C. and Peti, W. (2008) Detailed structural characterization of unbound protein phosphatase 1 inhibitors. Biochemistry 47, 12346-12356
    • (2008) Biochemistry , vol.47 , pp. 12346-12356
    • Dancheck, B.1    Nairn, A.C.2    Peti, W.3
  • 39
    • 0015528157 scopus 로고
    • Ligand binding and internal equilibria in proteins
    • Weber, G. (1972) Ligand binding and internal equilibria in proteins. Biochemistry 11, 864-878
    • (1972) Biochemistry , vol.11 , pp. 864-878
    • Weber, G.1
  • 40
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland, D.E. (1958) Application of a theory of enzyme specificity to protein synthesis. Proc. Natl. Acad. Sci. U.S.A. 44, 98-104
    • (1958) Proc. Natl. Acad. Sci. U.S.A. , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 41
    • 79960787160 scopus 로고    scopus 로고
    • Molecular basis for an ancient partnership between prolyl isomerase Pin1 and phosphatase inhibitor-2
    • Sami, F., Smet-Nocca, C., Khan, M., Landrieu, I., Lippens, G. and Brautigan, D.L. (2011) Molecular basis for an ancient partnership between prolyl isomerase Pin1 and phosphatase inhibitor-2. Biochemistry 50, 6567-6578
    • (2011) Biochemistry , vol.50 , pp. 6567-6578
    • Sami, F.1    Smet-Nocca, C.2    Khan, M.3    Landrieu, I.4    Lippens, G.5    Brautigan, D.L.6
  • 42
    • 0034808081 scopus 로고    scopus 로고
    • Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1
    • Connor, J.H., Weiser, D.C., Li, S., Hallenbeck, J.M. and Shenolikar, S. (2001) Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1. Mol. Cell. Biol. 21, 6841-6850
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6841-6850
    • Connor, J.H.1    Weiser, D.C.2    Li, S.3    Hallenbeck, J.M.4    Shenolikar, S.5
  • 43
    • 34547754412 scopus 로고    scopus 로고
    • A complex of catalytically inactive protein phosphatase-1 sandwiched between Sds22 and inhibitor-3
    • Lesage, B., Beullens, M., Pedelini, L., Garcia-Gimeno, M.A., Waelkens, E., Sanz, P. and Bollen, M. (2007) A complex of catalytically inactive protein phosphatase-1 sandwiched between Sds22 and inhibitor-3. Biochemistry 46, 8909-8919
    • (2007) Biochemistry , vol.46 , pp. 8909-8919
    • Lesage, B.1    Beullens, M.2    Pedelini, L.3    Garcia-Gimeno, M.A.4    Waelkens, E.5    Sanz, P.6    Bollen, M.7
  • 47
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H.J. and Wright, P.E. (2005) Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6, 197-208
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2


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