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Volumn 103, Issue 3, 2007, Pages 1053-1062

Cone arrestin binding to JNK3 and Mdm2: Conformational preference and localization of interaction sites

Author keywords

Arrestin; Cone photoreceptors; Nucleo cytoplasmic transport; Protein kinases; Protein protein interactions; Ubiquitin ligases

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE 10; PROTEIN MDM2; RETINA S ANTIGEN;

EID: 35248851130     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2007.04842.x     Document Type: Article
Times cited : (51)

References (56)
  • 1
    • 0032509524 scopus 로고    scopus 로고
    • The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP
    • Askjaer P., Jensen T. H., Nilsson J., Englmeier L. Kjems J (1998) The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP. J. Biol. Chem. 273, 33414 33422.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33414-33422
    • Askjaer, P.1    Jensen, T.H.2    Nilsson, J.3    Englmeier, L.4    Kjems, J.5
  • 3
    • 0030736417 scopus 로고    scopus 로고
    • A beta-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation
    • Barak L. S., Ferguson S. S., Zhang J. Caron M. G. (1997) A beta-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation. J. Biol. Chem. 272, 27497 27500.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27497-27500
    • Barak, L.S.1    Ferguson, S.S.2    Zhang, J.3    Caron, M.G.4
  • 6
    • 11144287167 scopus 로고    scopus 로고
    • GC1 deletion prevents light-dependent arrestin translocation in mouse cone photoreceptor cells
    • Coleman J. E. Semple-Rowland S. L. (2005) GC1 deletion prevents light-dependent arrestin translocation in mouse cone photoreceptor cells. Invest. Ophthalmol. Vis. Sci. 46, 12 16.
    • (2005) Invest. Ophthalmol. Vis. Sci. , vol.46 , pp. 12-16
    • Coleman, J.E.1    Semple-Rowland, S.L.2
  • 7
    • 0027939554 scopus 로고
    • Cone arrestin identified by targeting expression of a functional family
    • Craft C. M., Whitmore D. H. Wiechmann A. F. (1994) Cone arrestin identified by targeting expression of a functional family. J. Biol. Chem. 269, 4613 4619.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4613-4619
    • Craft, C.M.1    Whitmore, D.H.2    Wiechmann, A.F.3
  • 9
    • 14844328342 scopus 로고    scopus 로고
    • Temporal kinetics of the light/dark translocation and compartmentation of arrestin and alpha-transducin in mouse photoreceptor cells
    • Elias R. V., Sezate S. S., Cao W. McGinnis J. F. (2004) Temporal kinetics of the light/dark translocation and compartmentation of arrestin and alpha-transducin in mouse photoreceptor cells. Mol. Vis. 10, 672 681.
    • (2004) Mol. Vis. , vol.10 , pp. 672-681
    • Elias, R.V.1    Sezate, S.S.2    Cao, W.3    McGinnis, J.F.4
  • 10
    • 0030831534 scopus 로고    scopus 로고
    • CRM1 is responsible for intracellular transport mediated by the nuclear export signal
    • Fukuda M., Asano S., Nakamura T., Adachi M., Yoshida M., Yanagida M. Nishida E. (1997) CRM1 is responsible for intracellular transport mediated by the nuclear export signal. Nature 390, 308 311.
    • (1997) Nature , vol.390 , pp. 308-311
    • Fukuda, M.1    Asano, S.2    Nakamura, T.3    Adachi, M.4    Yoshida, M.5    Yanagida, M.6    Nishida, E.7
  • 11
    • 21644463635 scopus 로고    scopus 로고
    • β-Arrestin is crucial for ubiquitination and down-regulation of the insulin-like growth factor-1 receptor by acting as adaptor for the MDM2 E3 ligase
    • Girnita L., Shenoy S. K., Sehat B., Vasilcanu R., Girnita A., Lefkowitz R. J. Larsson O. (2005) β-Arrestin is crucial for ubiquitination and down-regulation of the insulin-like growth factor-1 receptor by acting as adaptor for the MDM2 E3 ligase. J. Biol. Chem. 280, 24412 24419.
    • (2005) J. Biol. Chem. , vol.280 , pp. 24412-24419
    • Girnita, L.1    Shenoy, S.K.2    Sehat, B.3    Vasilcanu, R.4    Girnita, A.5    Lefkowitz, R.J.6    Larsson, O.7
  • 13
    • 0027241013 scopus 로고
    • Visual arrestin interaction with rhodopsin: Sequential multisite binding ensures strict selectivity towards light-activated phosphorylated rhodopsin
    • Gurevich V. V. Benovic J. L. (1993) Visual arrestin interaction with rhodopsin: sequential multisite binding ensures strict selectivity towards light-activated phosphorylated rhodopsin. J. Biol. Chem. 268, 11628 11638.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11628-11638
    • Gurevich, V.V.1    Benovic, J.L.2
  • 14
    • 0034006773 scopus 로고    scopus 로고
    • Arrestin: Mutagenesis, expression, purification, and functional characterization
    • Gurevich V. V. Benovic J. L. (2000) Arrestin: mutagenesis, expression, purification, and functional characterization. Methods Enzymol. 315, 422 437.
    • (2000) Methods Enzymol. , vol.315 , pp. 422-437
    • Gurevich, V.V.1    Benovic, J.L.2
  • 15
    • 0041333148 scopus 로고    scopus 로고
    • The new face of active receptor bound arrestin attracts new partners
    • Gurevich V. V. Gurevich E. V. (2003) The new face of active receptor bound arrestin attracts new partners. Structure 11, 1037 1042.
    • (2003) Structure , vol.11 , pp. 1037-1042
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 16
    • 33845870964 scopus 로고    scopus 로고
    • Arrestins are ubiquitous regulators of cellular signaling pathways
    • Gurevich E. V. Gurevich V. V. (2006a) Arrestins are ubiquitous regulators of cellular signaling pathways. Genome Biol. 7, 236.
    • (2006) Genome Biol. , vol.7236
    • Gurevich, E.V.1    Gurevich, V.V.2
  • 17
    • 33646414189 scopus 로고    scopus 로고
    • The structural basis of arrestin-mediated regulation of G protein-coupled receptors
    • Gurevich V. V. Gurevich E. V. (2006b) The structural basis of arrestin-mediated regulation of G protein-coupled receptors. Pharm. Ther. 110, 465 502.
    • (2006) Pharm. Ther. , vol.110 , pp. 465-502
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 18
    • 0028322111 scopus 로고
    • Visual arrestin binding to rhodopsin: Intramolecular interaction between the basic N-terminus and acidic C-terminus of arrestin may regulate binding selectivity
    • Gurevich V. V., Chen C-Y., Kim C. M. Benovic J. L. (1994) Visual arrestin binding to rhodopsin: intramolecular interaction between the basic N-terminus and acidic C-terminus of arrestin may regulate binding selectivity. J. Biol. Chem. 269, 8721 8727.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8721-8727
    • Gurevich, V.V.1    Chen, C.-Y.2    Kim, C.M.3    Benovic, J.L.4
  • 19
    • 0028924953 scopus 로고
    • Arrestin interaction with G protein-coupled receptors. Direct binding studies of wild type and mutant arrestins with rhodopsin, b2-adrenergic, and m2 muscarinic cholinergic receptors
    • Gurevich V. V., Dion S. B., Onorato J. J., Ptasienski J., Kim C. M., Sterne-Marr R., Hosey M. M. Benovic J. L. (1995) Arrestin interaction with G protein-coupled receptors. Direct binding studies of wild type and mutant arrestins with rhodopsin, b2-adrenergic, and m2 muscarinic cholinergic receptors. J. Biol. Chem. 270, 720 731.
    • (1995) J. Biol. Chem. , vol.270 , pp. 720-731
    • Gurevich, V.V.1    Dion, S.B.2    Onorato, J.J.3    Ptasienski, J.4    Kim, C.M.5    Sterne-Marr, R.6    Hosey, M.M.7    Benovic, J.L.8
  • 20
    • 0034802172 scopus 로고    scopus 로고
    • Crystal structure of beta-arrestin at 1.9 Å: ppossible mechanism of receptor binding and membrane translocation
    • Han M., Gurevich V. V., Vishnivetskiy S. A., Sigler P. B. Schubert C. (2001) Crystal structure of beta-arrestin at 1.9 Å: possible mechanism of receptor binding and membrane translocation. Structure 9, 869 880.
    • (2001) Structure , vol.9 , pp. 869-880
    • Han, M.1    Gurevich, V.V.2    Vishnivetskiy, S.A.3    Sigler, P.B.4    Schubert, C.5
  • 21
  • 25
    • 0033574274 scopus 로고    scopus 로고
    • The 2.8 Å crystal structure of visual arrestin: A model for arrestin's regulation
    • Hirsch J. A., Schubert C., Gurevich V. V. Sigler P. B. (1999) The 2.8 Å crystal structure of visual arrestin: a model for arrestin's regulation. Cell 97, 257 269.
    • (1999) Cell , vol.97 , pp. 257-269
    • Hirsch, J.A.1    Schubert, C.2    Gurevich, V.V.3    Sigler, P.B.4
  • 26
    • 0141894860 scopus 로고    scopus 로고
    • Role of visual pigment properties in rod and cone phototransduction
    • Kefalov V., Fu Y., Marsh-Armstrong N. Yau K. W. (2003) Role of visual pigment properties in rod and cone phototransduction. Nature 425, 526 531.
    • (2003) Nature , vol.425 , pp. 526-531
    • Kefalov, V.1    Fu, Y.2    Marsh-Armstrong, N.3    Yau, K.W.4
  • 27
    • 0037163045 scopus 로고    scopus 로고
    • Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein-coupled receptor trafficking
    • Kim Y. M. Benovic J. L. (2002) Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein-coupled receptor trafficking. J. Biol. Chem. 277, 30760 30768.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30760-30768
    • Kim, Y.M.1    Benovic, J.L.2
  • 30
    • 17644402459 scopus 로고    scopus 로고
    • Transduction of receptor signals by beta-arrestins
    • Lefkowitz R. J. Shenoy S. K. (2005) Transduction of receptor signals by beta-arrestins. Science 308, 512 517.
    • (2005) Science , vol.308 , pp. 512-517
    • Lefkowitz, R.J.1    Shenoy, S.K.2
  • 33
    • 0035958940 scopus 로고    scopus 로고
    • Identification of a motif in the carboxyl terminus of beta-arrestin2 responsible for activation of JNK3
    • Miller W. E., McDonald P. H., Cai S. F., Field M. E., Davis R. J. Lefkowitz R. J. (2001) Identification of a motif in the carboxyl terminus of beta-arrestin2 responsible for activation of JNK3. J. Biol. Chem. 276, 27770 27777.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27770-27777
    • Miller, W.E.1    McDonald, P.H.2    Cai, S.F.3    Field, M.E.4    Davis, R.J.5    Lefkowitz, R.J.6
  • 34
    • 0027332380 scopus 로고
    • X-arrestin: A new retinal arrestin mapping to the X chromosome
    • Murakami A., Yajima T., Sakuma H., McLaren M. J. Inana G (1993) X-arrestin: a new retinal arrestin mapping to the X chromosome. FEBS Lett. 334, 203 209.
    • (1993) FEBS Lett. , vol.334 , pp. 203-209
    • Murakami, A.1    Yajima, T.2    Sakuma, H.3    McLaren, M.J.4    Inana, G.5
  • 35
    • 20444383209 scopus 로고    scopus 로고
    • Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions
    • Nair K. S., Hanson S. M., Mendez A. et al. (2005) Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions. Neuron 46, 555 567.
    • (2005) Neuron , vol.46 , pp. 555-567
    • Nair, K.S.1    Hanson, S.M.2    Mendez, A.3
  • 36
    • 33846834013 scopus 로고    scopus 로고
    • Targeting of diacylglycerol degradation to M1 muscarinic receptors by beta-arrestins
    • Nelson C. D., Perry S. J., Regier D. S., Prescott S. M., Topham M. K. Lefkowitz R. J. (2007) Targeting of diacylglycerol degradation to M1 muscarinic receptors by beta-arrestins. Science 315, 663 666.
    • (2007) Science , vol.315 , pp. 663-666
    • Nelson, C.D.1    Perry, S.J.2    Regier, D.S.3    Prescott, S.M.4    Topham, M.K.5    Lefkowitz, R.J.6
  • 37
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role of CRM1 in signal-mediated nuclear protein export
    • Ossareh-Nazari B., Bachelerie F. Dargemont C (1997) Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science 278, 141 144.
    • (1997) Science , vol.278 , pp. 141-144
    • Ossareh-Nazari, B.1    Bachelerie, F.2    Dargemont, C.3
  • 38
    • 0023650261 scopus 로고
    • Light-stimulated protein movement in rod photoreceptor cells of the rat retina
    • Philp N. J., Chang W. Long K (1987) Light-stimulated protein movement in rod photoreceptor cells of the rat retina. FEBS Lett. 225, 127 132.
    • (1987) FEBS Lett. , vol.225 , pp. 127-132
    • Philp, N.J.1    Chang, W.2    Long, K.3
  • 39
    • 0037020264 scopus 로고    scopus 로고
    • Differential nucleocytoplasmic shuttling of beta-arrestins. Characterization of a leucine-rich nuclear export signal in beta-arrestin2
    • Scott M. G., Le Rouzic E., Perianin A., Pierotti V., Enslen H., Benichou S., Marullo S. Benmerah A (2002) Differential nucleocytoplasmic shuttling of beta-arrestins. Characterization of a leucine-rich nuclear export signal in beta-arrestin2. J. Biol. Chem. 277, 37693 37701.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37693-37701
    • Scott, M.G.1    Le Rouzic, E.2    Perianin, A.3    Pierotti, V.4    Enslen, H.5    Benichou, S.6    Marullo, S.7    Benmerah, A.8
  • 40
    • 0037737763 scopus 로고    scopus 로고
    • Trafficking patterns of beta-arrestin and G protein-coupled receptors determined by the kinetics of beta-arrestin deubiquitination
    • Shenoy S. K. Lefkowitz R. J. (2003) Trafficking patterns of beta-arrestin and G protein-coupled receptors determined by the kinetics of beta-arrestin deubiquitination. J. Biol. Chem. 278, 14498 14506.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14498-14506
    • Shenoy, S.K.1    Lefkowitz, R.J.2
  • 41
    • 0035834428 scopus 로고    scopus 로고
    • Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin
    • Shenoy S. K., McDonald P. H., Kohout T. A. Lefkowitz R. J. (2001) Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin. Science 294, 1307 1313.
    • (2001) Science , vol.294 , pp. 1307-1313
    • Shenoy, S.K.1    McDonald, P.H.2    Kohout, T.A.3    Lefkowitz, R.J.4
  • 43
    • 33746351059 scopus 로고    scopus 로고
    • Visual and both non-visual arrestins in their 'inactive' conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm
    • Song X., Raman D., Gurevich E. V., Vishnivetskiy S. A. Gurevich V. V. (2006) Visual and both non-visual arrestins in their 'inactive' conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm. J. Biol. Chem. 281, 21491 21499.
    • (2006) J. Biol. Chem. , vol.281 , pp. 21491-21499
    • Song, X.1    Raman, D.2    Gurevich, E.V.3    Vishnivetskiy, S.A.4    Gurevich, V.V.5
  • 45
    • 32544453978 scopus 로고    scopus 로고
    • Arrestin translocation is induced at a critical threshold of visual signaling and is superstoichiometric to bleached rhodopsin
    • Strissel K. J., Sokolov M., Trieu L. H. Arshavsky V. Y. (2006) Arrestin translocation is induced at a critical threshold of visual signaling and is superstoichiometric to bleached rhodopsin. J. Neurosci. 26, 1146 1153.
    • (2006) J. Neurosci. , vol.26 , pp. 1146-1153
    • Strissel, K.J.1    Sokolov, M.2    Trieu, L.H.3    Arshavsky, V.Y.4
  • 47
    • 0037113983 scopus 로고    scopus 로고
    • Transition of arrestin in the active receptor-binding state requires an extended interdomain hinge
    • Vishnivetskiy S. A., Hirsch J. A., Velez M-G., Gurevich Y. V. Gurevich V. V. (2002) Transition of arrestin in the active receptor-binding state requires an extended interdomain hinge. J. Biol. Chem. 277, 43961 43968.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43961-43968
    • Vishnivetskiy, S.A.1    Hirsch, J.A.2    Velez, M.-G.3    Gurevich, Y.V.4    Gurevich, V.V.5
  • 48
    • 0038514264 scopus 로고    scopus 로고
    • Subcellular localization of beta-arrestins is determined by their intact N domain and the nuclear export signal at the C terminus
    • Wang P., Wu Y., Ge X., Ma L. Pei G (2003a) Subcellular localization of beta-arrestins is determined by their intact N domain and the nuclear export signal at the C terminus. J. Biol. Chem. 278, 11648 11653.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11648-11653
    • Wang, P.1    Wu, Y.2    Ge, X.3    Ma, L.4    Pei, G.5
  • 49
    • 0037458705 scopus 로고    scopus 로고
    • Beta-arrestin 2 functions as a G-protein-coupled receptor-activated regulator of oncoprotein Mdm2
    • Wang P., Gao H., Ni Y., Wang B., Wu Y., Ji L., Qin L., Ma L. Pei G. (2003b) Beta-arrestin 2 functions as a G-protein-coupled receptor-activated regulator of oncoprotein Mdm2. J. Biol. Chem. 278, 6363 6370.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6363-6370
    • Wang, P.1    Gao, H.2    Ni, Y.3    Wang, B.4    Wu, Y.5    Ji, L.6    Qin, L.7    Ma, L.8    Pei, G.9
  • 50
    • 0037459085 scopus 로고    scopus 로고
    • Regulating access to the genome: Nucleoplasmic transport throughout the cell cycle
    • Weis K (2003) Regulating access to the genome: nucleoplasmic transport throughout the cell cycle. Cell 112, 441 451.
    • (2003) Cell , vol.112 , pp. 441-451
    • Weis, K.1
  • 51
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • Wen W., Meinkoth J. L., Tsien R. Y. Taylor S. S. (1995) Identification of a signal for rapid export of proteins from the nucleus. Cell 82, 463 473.
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinkoth, J.L.2    Tsien, R.Y.3    Taylor, S.S.4
  • 53
    • 0038071520 scopus 로고    scopus 로고
    • Light-dependent redistribution of visual arrestins and transducin subunits in mice with defective phototransduction
    • Zhang H., Huang W., Zhu X., Craft C. M., Baehr W. Chen C. K. (2003) Light-dependent redistribution of visual arrestins and transducin subunits in mice with defective phototransduction. Mol. Vis. 9, 231 237.
    • (2003) Mol. Vis. , vol.9 , pp. 231-237
    • Zhang, H.1    Huang, W.2    Zhu, X.3    Craft, C.M.4    Baehr, W.5    Chen, C.K.6
  • 54
    • 0036978886 scopus 로고    scopus 로고
    • Mouse cone arrestin expression pattern: Light induced translocation in cone photoreceptors
    • Zhu X., Li A., Brown B., Weiss E. R., Osawa S. Craft C. M. (2002) Mouse cone arrestin expression pattern: light induced translocation in cone photoreceptors. Mol. Vis. 8, 462 471.
    • (2002) Mol. Vis. , vol.8 , pp. 462-471
    • Zhu, X.1    Li, A.2    Brown, B.3    Weiss, E.R.4    Osawa, S.5    Craft, C.M.6
  • 55
    • 0038825621 scopus 로고    scopus 로고
    • GRK1-dependent phosphorylation of S and M opsins and their binding to cone arrestin during cone phototransduction in the mouse retina
    • Zhu X., Brown B., Li A., Mears A. J., Swaroop A. Craft C. M. (2003) GRK1-dependent phosphorylation of S and M opsins and their binding to cone arrestin during cone phototransduction in the mouse retina. J. Neurosci. 23, 6152 6160.
    • (2003) J. Neurosci. , vol.23 , pp. 6152-6160
    • Zhu, X.1    Brown, B.2    Li, A.3    Mears, A.J.4    Swaroop, A.5    Craft, C.M.6


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