메뉴 건너뛰기




Volumn , Issue , 2012, Pages

Ubiquitin-mediated regulation of endocytosis by proteins of the arrestin family

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; EUKARYOTA; FUNGI; METAZOA;

EID: 84867025125     PISSN: 20902247     EISSN: 20902255     Source Type: Journal    
DOI: 10.1155/2012/242764     Document Type: Review
Times cited : (69)

References (116)
  • 1
    • 0000025689 scopus 로고
    • Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments
    • Wilden U., Hall S. W., Kuhn H., Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments. Proceedings of the National Academy of Sciences of the United States of America 1986 83 5 1174 1178 2-s2.0-0000025689 (Pubitemid 16016091)
    • (1986) Proceedings of the National Academy of Sciences of the United States of America , vol.83 , Issue.5 , pp. 1174-1178
    • Wilden, U.1    Hall, S.W.2    Kuhn, H.3
  • 2
    • 0022997189 scopus 로고
    • A 48 kDa protein arrests cGMP phosphodiesterase activation in retinal rod disk membranes
    • DOI 10.1016/0014-5793(86)80008-4
    • Zuckerman R., Cheasty J. E., A 48 kDa protein arrests cGMP phosphodiesterase activation in retinal rod disk membranes. FEBS Letters 1986 207 1 35 41 2-s2.0-0022997189 (Pubitemid 17179360)
    • (1986) FEBS Letters , vol.207 , Issue.1 , pp. 35-41
    • Zuckerman, R.1    Cheasty, J.E.2
  • 4
    • 0023515309 scopus 로고
    • Functional desensitization of the isolated β -adrenergic receptor by the beta-adrenergic receptor kinase: Potential role of an analog of the retinal protein arrestin (48-kDa protein)
    • 2-s2.0-0023515309
    • Benovic J. L., Kühn H., Weyand I., Codina J., Caron M. G., Lefkowitz R. J., Functional desensitization of the isolated β -adrenergic receptor by the beta-adrenergic receptor kinase: potential role of an analog of the retinal protein arrestin (48-kDa protein). Proceedings of the National Academy of Sciences of the United States of America 1987 84 24 8879 8882 2-s2.0-0023515309
    • (1987) Proceedings of the National Academy of Sciences of the United States of America , vol.84 , Issue.24 , pp. 8879-8882
    • Benovic, J.L.1    Kühn, H.2    Weyand, I.3    Codina, J.4    Caron, M.G.5    Lefkowitz, R.J.6
  • 5
    • 0025352299 scopus 로고
    • β -arrestin: A protein that regulates β -adrenergic receptor function
    • 2-s2.0-0025352299
    • Lohse M. J., Benovic J. L., Codina J., Cargon M. G., Lefkowitz R. J., β -arrestin: a protein that regulates β -adrenergic receptor function. Science 1990 248 4962 1547 1550 2-s2.0-0025352299
    • (1990) Science , vol.248 , Issue.4962 , pp. 1547-1550
    • Lohse, M.J.1    Benovic, J.L.2    Codina, J.3    Cargon, M.G.4    Lefkowitz, R.J.5
  • 7
    • 33947401068 scopus 로고    scopus 로고
    • β-Arrestins and cell signaling
    • DOI 10.1146/annurev.physiol.69.022405.154749
    • DeWire S. M., Ahn S., Lefkowitz R. J., Shenoy S. K., β -arrestins and cell signaling. Annual Review of Physiology 2007 69 483 510 2-s2.0-33947401068 10.1146/annurev.physiol.69.022405.154749 (Pubitemid 46457652)
    • (2007) Annual Review of Physiology , vol.69 , pp. 483-510
    • DeWire, S.M.1    Ahn, S.2    Lefkowitz, R.J.3    Shenoy, S.K.4
  • 8
    • 0842331059 scopus 로고    scopus 로고
    • The molecular acrobatics of arrestin activation
    • DOI 10.1016/j.tips.2003.12.008
    • Gurevich V. V., Gurevich E. V., The molecular acrobatics of arrestin activation. Trends in Pharmacological Sciences 2004 25 2 105 111 2-s2.0-0842331059 10.1016/j.tips.2003.12.008 (Pubitemid 38183397)
    • (2004) Trends in Pharmacological Sciences , vol.25 , Issue.2 , pp. 105-111
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 9
    • 41149090339 scopus 로고    scopus 로고
    • Regulation of GPCRs by endocytic membrane trafficking and its potential implications
    • DOI 10.1146/annurev.pharmtox.48.113006.094830
    • Hanyaloglu A. C., von Zastrow M., Regulation of GPCRs by endocytic membrane trafficking and its potential implications. Annual Review of Pharmacology and Toxicology 2008 48 537 568 2-s2.0-41149090339 10.1146/annurev.pharmtox.48.113006.094830 (Pubitemid 351738163)
    • (2008) Annual Review of Pharmacology and Toxicology , vol.48 , pp. 537-568
    • Hanyaloglu, A.C.1    Von Zastrow, M.2
  • 10
    • 33947314576 scopus 로고    scopus 로고
    • Regulation of receptor trafficking by GRKs and arrestins
    • DOI 10.1146/annurev.physiol.69.022405.154712
    • Moore C. A. C., Milano S. K., Benovic J. L., Regulation of receptor trafficking by GRKs and arrestins. Annual Review of Physiology 2007 69 451 482 2-s2.0-33947314576 10.1146/annurev.physiol.69.022405.154712 (Pubitemid 46457651)
    • (2007) Annual Review of Physiology , vol.69 , pp. 451-482
    • Moore, C.A.C.1    Milano, S.K.2    Benovic, J.L.3
  • 11
    • 0030967614 scopus 로고    scopus 로고
    • Arrestin/clathrin interaction. Localization of the clathrin binding domain of nonvisual arrestins to the carboxyl terminus
    • DOI 10.1074/jbc.272.23.15011
    • Krupnick J. G., Goodman O. B. Jr., Keen J. H., Benovic J. L., Arrestin/clathrin interaction. Localization of the clathrin binding domain of nonvisual arrestins to the carboxyl terminus. Journal of Biological Chemistry 1997 272 23 15011 15016 2-s2.0-0030967614 10.1074/jbc.272.23.15011 (Pubitemid 27251777)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.23 , pp. 15011-15016
    • Krupnick, J.G.1    Goodman Jr., O.B.2    Keen, J.H.3    Benovic, J.L.4
  • 13
    • 12644259509 scopus 로고    scopus 로고
    • Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain
    • DOI 10.1074/jbc.272.23.15017
    • Goodman O. B. Jr., Krupnick J. G., Gurevich V. V., Benovic J. L., Keen J. H., Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain. Journal of Biological Chemistry 1997 272 23 15017 15022 2-s2.0-12644259509 10.1074/jbc.272.23.15017 (Pubitemid 27251778)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.23 , pp. 15017-15022
    • Goodman Jr., O.B.1    Krupnick, J.G.2    Gurevich, V.V.3    Benovic, J.L.4    Keen, J.H.5
  • 14
    • 0037163045 scopus 로고    scopus 로고
    • Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein-coupled receptor trafficking
    • DOI 10.1074/jbc.M204528200
    • Kim Y. M., Benovic J. L., Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein-coupled receptor trafficking. Journal of Biological Chemistry 2002 277 34 30760 30768 2-s2.0-0037163045 10.1074/jbc.M204528200 (Pubitemid 34970773)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.34 , pp. 30760-30768
    • Kim, Y.-M.1    Benovic, J.L.2
  • 21
    • 77952415656 scopus 로고    scopus 로고
    • Beyond desensitization: Physiological relevance of arrestin-dependent signaling
    • 2-s2.0-77952415656 10.1124/pr.109.002436
    • Luttrell L. M., Gesty-Palmer D., Beyond desensitization: physiological relevance of arrestin-dependent signaling. Pharmacological Reviews 2010 62 2 305 330 2-s2.0-77952415656 10.1124/pr.109.002436
    • (2010) Pharmacological Reviews , vol.62 , Issue.2 , pp. 305-330
    • Luttrell, L.M.1    Gesty-Palmer, D.2
  • 22
    • 67349237981 scopus 로고    scopus 로고
    • Ubiquitin in trafficking: The network at work
    • 2-s2.0-67349237981 10.1016/j.yexcr.2008.10.014
    • Acconcia F., Sigismund S., Polo S., Ubiquitin in trafficking: the network at work. Experimental Cell Research 2009 315 9 1610 1618 2-s2.0-67349237981 10.1016/j.yexcr.2008.10.014
    • (2009) Experimental Cell Research , vol.315 , Issue.9 , pp. 1610-1618
    • Acconcia, F.1    Sigismund, S.2    Polo, S.3
  • 23
    • 84858129678 scopus 로고    scopus 로고
    • Signaling-mediated control of ubiquitin ligases in endocytosis
    • 10.1186/1741-7007-10-25
    • Polo S., Signaling-mediated control of ubiquitin ligases in endocytosis. BMC Biology 2012 10, article 25 10.1186/1741-7007-10-25
    • (2012) BMC Biology , vol.1025
    • Polo, S.1
  • 25
    • 49549116213 scopus 로고    scopus 로고
    • On the origins of arrestin and rhodopsin
    • ARTICLE 222 2-s2.0-49549116213 10.1186/1471-2148-8-222
    • Alvarez C. E., On the origins of arrestin and rhodopsin. BMC Evolutionary Biology 2008 8 1, article 222 2-s2.0-49549116213 10.1186/1471-2148-8-222
    • (2008) BMC Evolutionary Biology , vol.8 , Issue.1
    • Alvarez, C.E.1
  • 26
    • 65949089009 scopus 로고    scopus 로고
    • The arrestin fold: Variations on a theme
    • 2-s2.0-65949089009 10.2174/138920209787847014
    • Aubry L., Guetta D., Klein G., The arrestin fold: variations on a theme. Current Genomics 2009 10 2 133 142 2-s2.0-65949089009 10.2174/138920209787847014
    • (2009) Current Genomics , vol.10 , Issue.2 , pp. 133-142
    • Aubry, L.1    Guetta, D.2    Klein, G.3
  • 27
    • 55449109162 scopus 로고    scopus 로고
    • Finding the right partner: Science or ART?
    • 2-s2.0-55449109162 10.1016/j.cell.2008.10.032
    • Polo S., di Fiore P. P., Finding the right partner: science or ART? Cell 2008 135 4 590 592 2-s2.0-55449109162 10.1016/j.cell.2008.10.032
    • (2008) Cell , vol.135 , Issue.4 , pp. 590-592
    • Polo, S.1    Di Fiore, P.P.2
  • 28
    • 80052359992 scopus 로고    scopus 로고
    • Emerging paradigms of β -arrestin-dependent seven transmembrane receptor signaling
    • 2-s2.0-79960228625 10.1016/j.tibs.2011.06.003
    • Shukla A. K., Xiao K., Lefkowitz R. J., Emerging paradigms of β -arrestin-dependent seven transmembrane receptor signaling. Trends in Biochemical Sciences 2011 36 9 457 469 2-s2.0-79960228625 10.1016/j.tibs.2011. 06.003
    • (2011) Trends in Biochemical Sciences , vol.36 , Issue.9 , pp. 457-469
    • Shukla, A.K.1    Xiao, K.2    Lefkowitz, R.J.3
  • 29
    • 80052038573 scopus 로고    scopus 로고
    • β -arrestin-mediated receptor trafficking and signal transduction
    • 2-s2.0-79958294101 10.1016/j.tips.2011.05.002
    • Shenoy S. K., Lefkowitz R. J., β -arrestin-mediated receptor trafficking and signal transduction. Trends in Pharmacological Sciences 2011 32 9 521 533 2-s2.0-79958294101 10.1016/j.tips.2011.05.002
    • (2011) Trends in Pharmacological Sciences , vol.32 , Issue.9 , pp. 521-533
    • Shenoy, S.K.1    Lefkowitz, R.J.2
  • 30
    • 0035834428 scopus 로고    scopus 로고
    • 2-adrenergic receptor and β-arrestin
    • DOI 10.1126/science.1063866
    • 2-adrenergic receptor and β -arrestin. Science 2001 294 5545 1307 1313 2-s2.0-0035834428 10.1126/science.1063866 (Pubitemid 33063090)
    • (2001) Science , vol.294 , Issue.5545 , pp. 1307-1313
    • Shenoy, S.K.1    McDonald, P.H.2    Kohout, T.A.3    Lefkowitz, R.J.4
  • 32
    • 17144364766 scopus 로고    scopus 로고
    • Receptor-specific ubiquitination of β-arrestin directs assembly and targeting of seven-transmembrane receptor signalosomes
    • DOI 10.1074/jbc.M412418200
    • Shenoy S. K., Lefkowitz R. J., Receptor-specific ubiquitination of β -arrestin directs assembly and targeting of seven-transmembrane receptor signalosomes. Journal of Biological Chemistry 2005 280 15 15315 15324 2-s2.0-17144364766 10.1074/jbc.M412418200 (Pubitemid 40562888)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 15315-15324
    • Shenoy, S.K.1    Lefkowitz, R.J.2
  • 34
    • 55549102963 scopus 로고    scopus 로고
    • Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface
    • 2-s2.0-55549102963 10.1016/j.cell.2008.09.025
    • Lin C. H., MacGurn J. A., Chu T., Stefan C. J., Emr S. D., Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface. Cell 2008 135 4 714 725 2-s2.0-55549102963 10.1016/j.cell.2008.09.025
    • (2008) Cell , vol.135 , Issue.4 , pp. 714-725
    • Lin, C.H.1    MacGurn, J.A.2    Chu, T.3    Stefan, C.J.4    Emr, S.D.5
  • 36
    • 0037737763 scopus 로고    scopus 로고
    • Trafficking patterns of β-arrestin and G protein-coupled receptors determined by the kinetics of β-arrestin deubiquitination
    • DOI 10.1074/jbc.M209626200
    • Shenoy S. K., Lefkowitz R. J., Trafficking patterns of β -arrestin and G protein-coupled receptors determined by the kinetics of β -arrestin deubiquitination. Journal of Biological Chemistry 2003 278 16 14498 14506 2-s2.0-0037737763 10.1074/jbc.M209626200 (Pubitemid 36800003)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 14498-14506
    • Shenoy, S.K.1    Lefkowitz, R.J.2
  • 37
    • 67649556158 scopus 로고    scopus 로고
    • The deubiquitinases USP33 and USP20 coordinate β 2 adrenergic receptor recycling and resensitization
    • 2-s2.0-67649556158 10.1038/emboj.2009.128
    • Berthouze M., Venkataramanan V., Li Y., Shenoy S. K., The deubiquitinases USP33 and USP20 coordinate β 2 adrenergic receptor recycling and resensitization. The EMBO Journal 2009 28 12 1684 1696 2-s2.0-67649556158 10.1038/emboj.2009.128
    • (2009) The EMBO Journal , vol.28 , Issue.12 , pp. 1684-1696
    • Berthouze, M.1    Venkataramanan, V.2    Li, Y.3    Shenoy, S.K.4
  • 38
    • 0028277963 scopus 로고
    • The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants
    • Kolling R., Hollenberg C. P., The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants. The EMBO Journal 1994 13 14 3261 3271 2-s2.0-0028277963 (Pubitemid 24226940)
    • (1994) EMBO Journal , vol.13 , Issue.14 , pp. 3261-3271
    • Kolling, R.1    Hollenberg, C.P.2
  • 39
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • 2-s2.0-0030054178 10.1016/S0092-8674(00)80982-4
    • Hicke L., Riezman H., Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 1996 84 2 277 287 2-s2.0-0030054178 10.1016/S0092-8674(00)80982-4
    • (1996) Cell , vol.84 , Issue.2 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 40
    • 0029781462 scopus 로고    scopus 로고
    • Ubiquitination of the yeast a-factor receptor
    • Roth A. F., Davis N. G., Ubiquitination of the yeast a-factor receptor. Journal of Cell Biology 1996 134 3 661 674 2-s2.0-0029781462 (Pubitemid 26269139)
    • (1996) Journal of Cell Biology , vol.134 , Issue.3 , pp. 661-674
    • Roth, A.F.1    Davis, N.G.2
  • 41
    • 15844424064 scopus 로고    scopus 로고
    • Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease
    • DOI 10.1074/jbc.271.18.10946
    • Galan J. M., Moreau V., Andre B., Volland C., Haguenauer-Tsapis R., Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease. Journal of Biological Chemistry 1996 271 18 10946 10952 2-s2.0-15844424064 10.1074/jbc.271.18.10946 (Pubitemid 26145835)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.18 , pp. 10946-10952
    • Galan, J.M.1    Moreau, V.2    Andre, B.3    Volland, C.4    Haguenauer-Tsapis, R.5
  • 42
    • 77950857969 scopus 로고    scopus 로고
    • The ubiquitin code of yeast permease trafficking
    • 2-s2.0-77950857969 10.1016/j.tcb.2010.01.004
    • Lauwers E., Erpapazoglou Z., Haguenauer-Tsapis R., André B., The ubiquitin code of yeast permease trafficking. Trends in Cell Biology 2010 20 4 196 204 2-s2.0-77950857969 10.1016/j.tcb.2010.01.004
    • (2010) Trends in Cell Biology , vol.20 , Issue.4 , pp. 196-204
    • Lauwers, E.1    Erpapazoglou, Z.2    Haguenauer-Tsapis, R.3    André, B.4
  • 43
    • 58149311474 scopus 로고    scopus 로고
    • Opposing activities of the snx3-retromer complex and ESCRT proteins mediate regulated cargo sorting at a common endosome
    • 2-s2.0-58149311474 10.1091/mbc.E08-03-0296
    • Strochlic T. I., Schmiedekamp B. C., Lee J., Katzmann D. J., Burd C. G., Opposing activities of the snx3-retromer complex and ESCRT proteins mediate regulated cargo sorting at a common endosome. Molecular Biology of the Cell 2008 19 11 4694 4706 2-s2.0-58149311474 10.1091/mbc.E08-03-0296
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.11 , pp. 4694-4706
    • Strochlic, T.I.1    Schmiedekamp, B.C.2    Lee, J.3    Katzmann, D.J.4    Burd, C.G.5
  • 44
    • 69249135065 scopus 로고    scopus 로고
    • Tickets to ride: Selecting cargo for clathrin-regulated internalization
    • 2-s2.0-69249135065 10.1038/nrm2751
    • Traub L. M., Tickets to ride: selecting cargo for clathrin-regulated internalization. Nature Reviews Molecular Cell Biology 2009 10 9 583 596 2-s2.0-69249135065 10.1038/nrm2751
    • (2009) Nature Reviews Molecular Cell Biology , vol.10 , Issue.9 , pp. 583-596
    • Traub, L.M.1
  • 45
    • 0036094688 scopus 로고    scopus 로고
    • Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis
    • DOI 10.1038/ncb790
    • Shih S. C., Katzmann D. J., Schnell J. D., Sutanto M., Emr S. D., Hicke L., Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. Nature Cell Biology 2002 4 5 389 393 2-s2.0-0036094688 10.1038/ncb790 (Pubitemid 34521036)
    • (2002) Nature Cell Biology , vol.4 , Issue.5 , pp. 389-393
    • Shih, S.C.1    Katzmann, D.J.2    Schnell, J.D.3    Sutanto, M.4    Emr, S.D.5    Hicke, L.6
  • 46
    • 0037518120 scopus 로고    scopus 로고
    • The yeast epsin Ent1 is recruited to membranes through multiple independent interactions
    • DOI 10.1074/jbc.M211622200
    • Aguilar R. C., Watson H. A., Wendland B., The yeast epsin Ent1 is recruited to membranes through multiple independent interactions. Journal of Biological Chemistry 2003 278 12 10737 10743 2-s2.0-0037518120 10.1074/jbc.M211622200 (Pubitemid 36800345)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.12 , pp. 10737-10743
    • Claudio Aguilar, R.1    Watson, H.A.2    Wendland, B.3
  • 47
    • 33644529627 scopus 로고    scopus 로고
    • Molecular basis of oligoubiquitin-dependent internalization of membrane proteins in mammalian cells
    • DOI 10.1111/j.1600-0854.2006.00384.x
    • Barriere H., Nemes C., Lechardeur D., Khan-Mohammad M., Fruh K., Lukacs G. L., Molecular basis of oligoubiquitin-dependent internalization of membrane proteins in mammalian cells. Traffic 2006 7 3 282 297 2-s2.0-33644529627 10.1111/j.1600-0854.2006.00384.x (Pubitemid 43323956)
    • (2006) Traffic , vol.7 , Issue.3 , pp. 282-297
    • Barriere, H.1    Nemes, C.2    Lechardeur, D.3    Khan-Mohammad, M.4    Fruh, K.5    Lukacs, G.L.6
  • 48
    • 58549096725 scopus 로고    scopus 로고
    • Epsin 1 is involved in recruitment of ubiquitinated EGF receptors into clathrin-coated pits
    • 2-s2.0-58549096725 10.1111/j.1600-0854.2008.00858.x
    • Kazazic M., Bertelsen V., Pedersen K. W., Vuong T. T., Grandal M. V., Rodland M. S., Traub L. M., Stang E., Madshus I. H., Epsin 1 is involved in recruitment of ubiquitinated EGF receptors into clathrin-coated pits. Traffic 2009 10 2 235 245 2-s2.0-58549096725 10.1111/j.1600-0854.2008.00858.x
    • (2009) Traffic , vol.10 , Issue.2 , pp. 235-245
    • Kazazic, M.1    Bertelsen, V.2    Pedersen, K.W.3    Vuong, T.T.4    Grandal, M.V.5    Rodland, M.S.6    Traub, L.M.7    Stang, E.8    Madshus, I.H.9
  • 50
    • 71849101657 scopus 로고    scopus 로고
    • The function of yeast epsin and Ede1 ubiquitin-binding domains during receptor internalization
    • 2-s2.0-71849101657 10.1111/j.1600-0854.2009.01003.x
    • Dores M. R., Schnell J. D., Maldonado-Baez L., Wendland B., Hicke L., The function of yeast epsin and Ede1 ubiquitin-binding domains during receptor internalization. Traffic 2010 11 1 151 160 2-s2.0-71849101657 10.1111/j.1600-0854.2009.01003.x
    • (2010) Traffic , vol.11 , Issue.1 , pp. 151-160
    • Dores, M.R.1    Schnell, J.D.2    Maldonado-Baez, L.3    Wendland, B.4    Hicke, L.5
  • 51
    • 0037125983 scopus 로고    scopus 로고
    • Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors
    • 2-s2.0-0037125983 10.1073/pnas.192462299
    • Haglund K., Shimokawa N., Szymkiewicz I., Dikic I., Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors. Proceedings of the National Academy of Sciences of the United States of America 2002 99 19 12191 12196 2-s2.0-0037125983 10.1073/pnas.192462299
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.19 , pp. 12191-12196
    • Haglund, K.1    Shimokawa, N.2    Szymkiewicz, I.3    Dikic, I.4
  • 52
    • 18544383164 scopus 로고    scopus 로고
    • Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and Hgs, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by Nedd4
    • 2-s2.0-18544383164 10.1034/j.1600-0854.2002.31006.x
    • Katz M., Shtiegman K., Tal-Or P., Yakir L., Mosesson Y., Harari D., Machluf Y., Asao H., Jovin T., Sugamura K., Yarden Y., Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and Hgs, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by Nedd4. Traffic 2002 3 10 740 751 2-s2.0-18544383164 10.1034/j.1600-0854.2002. 31006.x
    • (2002) Traffic , vol.3 , Issue.10 , pp. 740-751
    • Katz, M.1    Shtiegman, K.2    Tal-Or, P.3    Yakir, L.4    Mosesson, Y.5    Harari, D.6    MacHluf, Y.7    Asao, H.8    Jovin, T.9    Sugamura, K.10    Yarden, Y.11
  • 53
    • 0037187597 scopus 로고    scopus 로고
    • A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins
    • DOI 10.1038/416451a
    • Polo S., Sigismund S., Faretta M., Guidi M., Capua M. R., Bossi G., Chen H., De Camilli P., Di Fiore P. P., A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins. Nature 2002 416 6879 451 455 2-s2.0-0037187597 10.1038/416451a (Pubitemid 34272882)
    • (2002) Nature , vol.416 , Issue.6879 , pp. 451-455
    • Polo, S.1    Sigismund, S.2    Faretta, M.3    Guidi, M.4    Capua, M.R.5    Bossi, G.6    Chen, H.7    De Camilli, P.8    Di Fiore, P.P.9
  • 54
    • 80052621127 scopus 로고    scopus 로고
    • How Ubiquitin Functions with ESCRTs
    • 2-s2.0-79960681789 10.1111/j.1600-0854.2011.01242.x
    • Shields S. B., Piper R. C., How Ubiquitin Functions with ESCRTs. Traffic 2011 12 10 1306 1317 2-s2.0-79960681789 10.1111/j.1600-0854.2011.01242.x
    • (2011) Traffic , vol.12 , Issue.10 , pp. 1306-1317
    • Shields, S.B.1    Piper, R.C.2
  • 55
    • 79960225411 scopus 로고    scopus 로고
    • The ESCRT pathway
    • 2-s2.0-79960225411 10.1016/j.devcel.2011.05.015
    • Henne W. M., Buchkovich N. J., Emr S. D., The ESCRT pathway. Developmental Cell 2011 21 1 77 91 2-s2.0-79960225411 10.1016/j.devcel.2011.05. 015
    • (2011) Developmental Cell , vol.21 , Issue.1 , pp. 77-91
    • Henne, W.M.1    Buchkovich, N.J.2    Emr, S.D.3
  • 56
    • 0036902646 scopus 로고    scopus 로고
    • Receptor downregulation and multivesicular-body sorting
    • DOI 10.1038/nrm973
    • Katzmann D. J., Odorizzi G., Emr S. D., Receptor downregulation and multivesicular-body sorting. Nature Reviews Molecular Cell Biology 2002 3 12 893 905 2-s2.0-0036902646 10.1038/nrm973 (Pubitemid 35477368)
    • (2002) Nature Reviews Molecular Cell Biology , vol.3 , Issue.12 , pp. 893-905
    • Katzmann, D.J.1    Odorizzi, G.2    Emr, S.D.3
  • 57
    • 0029765099 scopus 로고    scopus 로고
    • The ubiquitin conjugation system is required for ligand-induced endocytosis and degradation of the growth hormone receptor
    • Strous G. J., van Kerkhof P., Govers R., Ciechanover A., Schwartz A. L., The ubiquitin conjugation system is required for ligand-induced endocytosis and degradation of the growth hormone receptor. The EMBO Journal 1996 15 15 3806 3812 2-s2.0-0029765099 (Pubitemid 26289790)
    • (1996) EMBO Journal , vol.15 , Issue.15 , pp. 3806-3812
    • Strous, G.J.1    Van Kerkhof, P.2    Govers, R.3    Ciechanover, A.4    Schwartz, A.L.5
  • 59
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of Membrane Protein Transport by Ubiquitin and Ubiquitin-Binding Proteins
    • DOI 10.1146/annurev.cellbio.19.110701.154617
    • Hicke L., Dunn R., Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annual Review of Cell and Developmental Biology 2003 19 141 172 2-s2.0-0141442586 10.1146/annurev.cellbio.19.110701.154617 (Pubitemid 37487346)
    • (2003) Annual Review of Cell and Developmental Biology , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 60
    • 33846471122 scopus 로고    scopus 로고
    • Proteasome-independent functions of ubiquitin in endocytosis and signaling
    • DOI 10.1126/science.1127085
    • Mukhopadhyay D., Riezman H., Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science 2007 315 5809 201 205 2-s2.0-33846471122 10.1126/science.1127085 (Pubitemid 46166358)
    • (2007) Science , vol.315 , Issue.5809 , pp. 201-205
    • Mukhopadhyay, D.1    Riezman, H.2
  • 61
    • 78651092657 scopus 로고    scopus 로고
    • Role of ubiquitination in endocytic trafficking of G-protein-coupled receptors
    • 2-s2.0-78651092657 10.1111/j.1600-0854.2010.01121.x
    • Hislop J. N., von Zastrow M., Role of ubiquitination in endocytic trafficking of G-protein-coupled receptors. Traffic 2011 12 2 137 148 2-s2.0-78651092657 10.1111/j.1600-0854.2010.01121.x
    • (2011) Traffic , vol.12 , Issue.2 , pp. 137-148
    • Hislop, J.N.1    Von Zastrow, M.2
  • 62
    • 23844436643 scopus 로고    scopus 로고
    • Caveolae: Stable membrane domains with a potential for internalization
    • DOI 10.1111/j.1600-0854.2005.00314.x
    • Hommelgaard A. M., Roepstorff K., Vilhardt F., Torgersen M. L., Sandvig K., van Deurs B., Caveolae: stable membrane domains with a potential for internalization. Traffic 2005 6 9 720 724 2-s2.0-23844436643 10.1111/j.1600-0854.2005.00314.x (Pubitemid 41179405)
    • (2005) Traffic , vol.6 , Issue.9 , pp. 720-724
    • Hommelgaard, A.M.1    Roepstorff, K.2    Vilhardt, F.3    Torgersen, M.L.4    Sandvig, K.5    Van Deurs, B.6
  • 63
    • 0035824563 scopus 로고    scopus 로고
    • Agonist-promoted ubiquitination of the G protein-coupled receptor CXCR4 mediates lysosomal sorting
    • 2-s2.0-0035824563 10.1074/jbc.C100527200
    • Marchese A., Benovic J. L., Agonist-promoted ubiquitination of the G protein-coupled receptor CXCR4 mediates lysosomal sorting. Journal of Biological Chemistry 2001 276 49 45509 45512 2-s2.0-0035824563 10.1074/jbc.C100527200
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.49 , pp. 45509-45512
    • Marchese, A.1    Benovic, J.L.2
  • 64
    • 77956919285 scopus 로고    scopus 로고
    • Arresting a transient receptor potential (TRP) channel: β -arrestin 1 mediates ubiquitination and functional down-regulation of TRPV4
    • 2-s2.0-77956919285 10.1074/jbc.M110.141549
    • Shukla A. K., Kim J., Ahn S., Xiao K., Shenoy S. K., Liedtke W., Lefkowitz R. J., Arresting a transient receptor potential (TRP) channel: β -arrestin 1 mediates ubiquitination and functional down-regulation of TRPV4. Journal of Biological Chemistry 2010 285 39 30115 30125 2-s2.0-77956919285 10.1074/jbc.M110.141549
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.39 , pp. 30115-30125
    • Shukla, A.K.1    Kim, J.2    Ahn, S.3    Xiao, K.4    Shenoy, S.K.5    Liedtke, W.6    Lefkowitz, R.J.7
  • 65
    • 78649673808 scopus 로고    scopus 로고
    • + exchanger 1 ubiquitylation, endocytosis, and function
    • 2-s2.0-78649673808 10.1074/jbc.M110.115089
    • + exchanger 1 ubiquitylation, endocytosis, and function. Journal of Biological Chemistry 2010 285 49 38293 38303 2-s2.0-78649673808 10.1074/jbc.M110.115089
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.49 , pp. 38293-38303
    • Simonin, A.1    Fuster, D.2
  • 66
    • 0242362743 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase AIP4 mediates ubiquitination and sorting of the G protein-coupled receptor CXCR4
    • DOI 10.1016/S1534-5807(03)00321-6, PII S1534580703003216
    • Marchese A., Raiborg C., Santini F., Keen J. H., Stenmark H., Benovic J. L., The E3 ubiquitin ligase AIP4 mediates ubiquitination and sorting of the G protein-coupled receptor CXCR4. Developmental Cell 2003 5 5 709 722 2-s2.0-0242362743 10.1016/S1534-5807(03)00321-6 (Pubitemid 37362215)
    • (2003) Developmental Cell , vol.5 , Issue.5 , pp. 709-722
    • Marchese, A.1    Raiborg, C.2    Santini, F.3    Keen, J.H.4    Stenmark, H.5    Benovic, J.L.6
  • 67
    • 37549035071 scopus 로고    scopus 로고
    • Arrestin-2 interacts with the ubiquitin-protein isopeptide ligase atrophin-interacting protein 4 and mediates endosomal sorting of the chemokine receptor CXCR4
    • 2-s2.0-37549035071 10.1074/jbc.M705085200
    • Bhandari D., Trejo J., Benovic J. L., Marchese A., Arrestin-2 interacts with the ubiquitin-protein isopeptide ligase atrophin-interacting protein 4 and mediates endosomal sorting of the chemokine receptor CXCR4. Journal of Biological Chemistry 2007 282 51 36971 36979 2-s2.0-37549035071 10.1074/jbc.M705085200
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.51 , pp. 36971-36979
    • Bhandari, D.1    Trejo, J.2    Benovic, J.L.3    Marchese, A.4
  • 68
    • 65249115360 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase atrophin interacting protein 4 binds directly to the chemokine receptor CXCR4 via a novel WW domain-mediated interaction
    • 2-s2.0-65249115360 10.1091/mbc.E08-03-0308
    • Bhandari D., Robia S. L., Marchese A., The E3 ubiquitin ligase atrophin interacting protein 4 binds directly to the chemokine receptor CXCR4 via a novel WW domain-mediated interaction. Molecular Biology of the Cell 2009 20 5 1324 1339 2-s2.0-65249115360 10.1091/mbc.E08-03-0308
    • (2009) Molecular Biology of the Cell , vol.20 , Issue.5 , pp. 1324-1339
    • Bhandari, D.1    Robia, S.L.2    Marchese, A.3
  • 69
    • 77954626403 scopus 로고    scopus 로고
    • Arrestin-2 interacts with the endosomal sorting complex required for transport machinery to modulate endosomal sorting of CXCR4
    • 2-s2.0-77954626403 10.1091/mbc.E10-02-0169
    • Malik R., Marchese A., Arrestin-2 interacts with the endosomal sorting complex required for transport machinery to modulate endosomal sorting of CXCR4. Molecular Biology of the Cell 2010 21 14 2529 2541 2-s2.0-77954626403 10.1091/mbc.E10-02-0169
    • (2010) Molecular Biology of the Cell , vol.21 , Issue.14 , pp. 2529-2541
    • Malik, R.1    Marchese, A.2
  • 71
    • 67349113489 scopus 로고    scopus 로고
    • Ubiquitin ligase adaptors: Regulators of ubiquitylation and endocytosis of plasma membrane proteins
    • 2-s2.0-67349113489 10.1016/j.yexcr.2008.11.014
    • Léon S., Haguenauer-Tsapis R., Ubiquitin ligase adaptors: regulators of ubiquitylation and endocytosis of plasma membrane proteins. Experimental Cell Research 2009 315 9 1574 1583 2-s2.0-67349113489 10.1016/j.yexcr.2008.11.014
    • (2009) Experimental Cell Research , vol.315 , Issue.9 , pp. 1574-1583
    • Léon, S.1    Haguenauer-Tsapis, R.2
  • 72
    • 0033610892 scopus 로고    scopus 로고
    • β-Arrestins regulate mitogenic signaling and clathrin-mediated endocytosis of the insulin-like growth factor I receptor
    • DOI 10.1074/jbc.273.48.31640
    • Lin F. T., Daaka Y., Lefkowitz R. J., β -arrestins regulate mitogenic signaling and clathrin-mediated endocytosis of the insulin-like growth factor I receptor. Journal of Biological Chemistry 1998 273 48 31640 31643 2-s2.0-0033610892 10.1074/jbc.273.48.31640 (Pubitemid 29177090)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.48 , pp. 31640-31643
    • Lin, F.-T.1    Daaka, Y.2    Lefkowitz, R.J.3
  • 73
    • 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
    • DOI 10.1074/jbc.M501129200
    • Girnita L., Shenoy S. K., Sehat B., Vasilcanu R., Girnita A., Lefkowitz R. J., Larsson O., 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. Journal of Biological Chemistry 2005 280 26 24412 24419 2-s2.0-21644463635 10.1074/jbc.M501129200 (Pubitemid 40934525)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , 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
  • 75
    • 0032568021 scopus 로고    scopus 로고
    • X-ray crystal structure of arrestin from bovine rod outer segments
    • DOI 10.1038/36147
    • Granzin J., Wilden U., Choe H. W., Labahn J., Krafft B., Buldt G., X-ray crystal structure of arrestin from bovine rod outer segments. Nature 1998 391 6670 918 921 2-s2.0-0032568021 10.1038/36147 (Pubitemid 28157673)
    • (1998) Nature , vol.391 , Issue.6670 , pp. 918-921
    • Granzin, J.1    Wilden, U.2    Choe, H.-W.3    Labahn, J.4    Krafft, B.5    Buldt, G.6
  • 76
    • 0034802172 scopus 로고    scopus 로고
    • Crystal structure of β-arrestin at 1.9 A: Possible mechanism of receptor binding and membrane translocation
    • DOI 10.1016/S0969-2126(01)00644-X, PII S096921260100644X
    • Han M., Gurevich V. V., Vishnivetskiy S. A., Sigler P. B., Schubert C., Crystal structure of β -arrestin at 1.9 Å: possible mechanism of receptor binding and membrane translocation. Structure 2001 9 9 869 880 2-s2.0-0034802172 10.1016/S0969-2126(01)00644-X (Pubitemid 32913504)
    • (2001) Structure , vol.9 , Issue.9 , pp. 869-880
    • Han, M.1    Gurevich, V.V.2    Vishnivetskiy, S.A.3    Sigler, P.B.4    Schubert, C.5
  • 77
    • 0033574274 scopus 로고    scopus 로고
    • The 2.8 Å crystal structure of visual arrestin: A model for arrestin's regulation
    • 2-s2.0-0033574274
    • Hirsch J. A., Schubert C., Gurevich V. V., Sigler P. B., The 2.8 Å crystal structure of visual arrestin: a model for arrestin's regulation. Cell 1999 97 2 257 269 2-s2.0-0033574274
    • (1999) Cell , vol.97 , Issue.2 , pp. 257-269
    • Hirsch, J.A.1    Schubert, C.2    Gurevich, V.V.3    Sigler, P.B.4
  • 78
    • 0037066145 scopus 로고    scopus 로고
    • Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis
    • DOI 10.1021/bi015905j
    • Milano S. K., Pace H. C., Kim Y. M., Brenner C., Benovic J. L., Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis. Biochemistry 2002 41 10 3321 3328 2-s2.0-0037066145 10.1021/bi015905j (Pubitemid 34214030)
    • (2002) Biochemistry , vol.41 , Issue.10 , pp. 3321-3328
    • Milano, S.K.1    Pace, H.C.2    Kim, Y.-M.3    Brenner, C.4    Benovic, J.L.5
  • 79
    • 33646942810 scopus 로고    scopus 로고
    • Nonvisual arrestin oligomerization and cellular localization are regulated by inositol hexakisphosphate binding
    • DOI 10.1074/jbc.M512703200
    • Milano S. K., Kim Y. M., Stefano F. P., Benovic J. L., Brenner C., Nonvisual arrestin oligomerization and cellular localization are regulated by inositol hexakisphosphate binding. Journal of Biological Chemistry 2006 281 14 9812 9823 2-s2.0-33646942810 10.1074/jbc.M512703200 (Pubitemid 43864700)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.14 , pp. 9812-9823
    • Milano, S.K.1    Kim, Y.-M.2    Stefano, F.P.3    Benovic, J.L.4    Brenner, C.5
  • 81
    • 33744943284 scopus 로고    scopus 로고
    • The retromer subunit Vps26 has an arrestin fold and binds Vps35 through its C-terminal domain
    • DOI 10.1038/nsmb1103, PII N1103
    • Shi H., Rojas R., Bonifacino J. S., Hurley J. H., The retromer subunit Vps26 has an arrestin fold and binds Vps35 through its C-terminal domain. Nature Structural and Molecular Biology 2006 13 6 540 548 2-s2.0-33744943284 10.1038/nsmb1103 (Pubitemid 43848909)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.6 , pp. 540-548
    • Shi, H.1    Rojas, R.2    Bonifacino, J.S.3    Hurley, J.H.4
  • 82
    • 38849094724 scopus 로고    scopus 로고
    • Structure of Vps26B and mapping of its interaction with the retromer protein complex
    • DOI 10.1111/j.1600-0854.2007.00688.x
    • Collins B. M., Norwood S. J., Kerr M. C., Mahony D., Seaman M. N. J., Teasdale R. D., Owen D. J., Structure of Vps26B and mapping of its interaction with the retromer protein complex. Traffic 2008 9 3 366 379 2-s2.0-38849094724 10.1111/j.1600-0854.2007.00688.x (Pubitemid 351188996)
    • (2008) Traffic , vol.9 , Issue.3 , pp. 366-379
    • Collins, B.M.1    Norwood, S.J.2    Kerr, M.C.3    Mahony, D.4    Seaman, M.N.J.5    Teasdale, R.D.6    Owen, D.J.7
  • 83
    • 3843055866 scopus 로고    scopus 로고
    • A role for creD, a carbon catabolite repression gene from Aspergillus nidulans, in ubiquitination
    • DOI 10.1111/j.1365-2958.2004.04172.x
    • Boase N. A., Kelly J. M., A role for creD, a carbon catabolite repression gene from Aspergillus nidulans, in ubiquitination. Molecular Microbiology 2004 53 3 929 940 2-s2.0-3843055866 10.1111/j.1365-2958.2004.04172.x (Pubitemid 39036970)
    • (2004) Molecular Microbiology , vol.53 , Issue.3 , pp. 929-940
    • Boase, N.A.1    Kelly, J.M.2
  • 84
    • 70649112359 scopus 로고    scopus 로고
    • Arrestin-mediated endocytosis of yeast plasma membrane transporters
    • 2-s2.0-70649112359 10.1111/j.1600-0854.2009.00990.x
    • Nikko E., Pelham H. R. B., Arrestin-mediated endocytosis of yeast plasma membrane transporters. Traffic 2009 10 12 1856 1867 2-s2.0-70649112359 10.1111/j.1600-0854.2009.00990.x
    • (2009) Traffic , vol.10 , Issue.12 , pp. 1856-1867
    • Nikko, E.1    Pelham, H.R.B.2
  • 85
    • 57049101734 scopus 로고    scopus 로고
    • Arrestin-like proteins mediate ubiquitination and endocytosis of the yeast metal transporter Smf1
    • 2-s2.0-57049101734 10.1038/embor.2008.199
    • Nikko E., Sullivan J. A., Pelham H. R. B., Arrestin-like proteins mediate ubiquitination and endocytosis of the yeast metal transporter Smf1. EMBO Reports 2008 9 12 1216 1221 2-s2.0-57049101734 10.1038/embor.2008.199
    • (2008) EMBO Reports , vol.9 , Issue.12 , pp. 1216-1221
    • Nikko, E.1    Sullivan, J.A.2    Pelham, H.R.B.3
  • 86
    • 0037077728 scopus 로고    scopus 로고
    • PY motifs of Rod1 are required for binding to Rsp5 and for drug resistance
    • 2-s2.0-0037077728 10.1016/S0014-5793(02)03104-6
    • Andoh T., Hirata Y., Kikuchi A., PY motifs of Rod1 are required for binding to Rsp5 and for drug resistance. FEBS Letters 2002 525 13 131 134 2-s2.0-0037077728 10.1016/S0014-5793(02)03104-6
    • (2002) FEBS Letters , vol.525 , Issue.13 , pp. 131-134
    • Andoh, T.1    Hirata, Y.2    Kikuchi, A.3
  • 87
    • 33845970909 scopus 로고    scopus 로고
    • 63-linked polyubiquitin conjugates in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.M608756200
    • 63-linked polyubiquitin conjugates in Saccharomyces cerevisiae. Journal of Biological Chemistry 2006 281 48 36724 36731 2-s2.0-33845970909 10.1074/jbc.M608756200 (Pubitemid 46042139)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.48 , pp. 36724-36731
    • Kee, Y.1    Munoz, W.2    Lyon, N.3    Huibregtse, J.M.4
  • 88
    • 34249947558 scopus 로고    scopus 로고
    • Ubiquitination screen using protein microarrays for comprehensive identification of Rsp5 substrates in yeast
    • DOI 10.1038/msb4100159, PII MSB4100159
    • Gupta R., Kus B., Fladd C., Wasmuth J., Tonikian R., Sidhu S., Krogan N. J., Parkinson J., Rotin D., Ubiquitination screen using protein microarrays for comprehensive identification of Rsp5 substrates in yeast. Molecular Systems Biology 2007 3, article 116 2-s2.0-34249947558 10.1038/msb4100159 (Pubitemid 46878941)
    • (2007) Molecular Systems Biology , vol.3 , pp. 116
    • Gupta, R.1    Kus, B.2    Fladd, C.3    Wasmuth, J.4    Tonikian, R.5    Sidhu, S.6    Krogan, N.J.7    Parkinson, J.8    Rotin, D.9
  • 89
    • 75749137330 scopus 로고    scopus 로고
    • Recruitment of the ESCRT machinery to a putative seven-transmembrane- domain receptor is mediated by an arrestin-related protein
    • 2-s2.0-75749137330 10.1128/MCB.00132-09
    • Herrador A., Herranz S., Lara D., Vincent O., Recruitment of the ESCRT machinery to a putative seven-transmembrane-domain receptor is mediated by an arrestin-related protein. Molecular and Cellular Biology 2010 30 4 897 907 2-s2.0-75749137330 10.1128/MCB.00132-09
    • (2010) Molecular and Cellular Biology , vol.30 , Issue.4 , pp. 897-907
    • Herrador, A.1    Herranz, S.2    Lara, D.3    Vincent, O.4
  • 90
    • 80052416211 scopus 로고    scopus 로고
    • Endocytosis of the aspartic acid/glutamic acid transporter Dip5 is triggered by substrate-dependent recruitment of the Rsp5 ubiquitin ligase via the arrestin-like protein Aly2
    • 10.1128/MCB.00464-10
    • Hatakeyama R., Kamiya M., Takahara T., Maeda T., Endocytosis of the aspartic acid/glutamic acid transporter Dip5 is triggered by substrate-dependent recruitment of the Rsp5 ubiquitin ligase via the arrestin-like protein Aly2. Molecular and Cellular Biology 2010 30 24 5598 5607 10.1128/MCB.00464-10
    • (2010) Molecular and Cellular Biology , vol.30 , Issue.24 , pp. 5598-5607
    • Hatakeyama, R.1    Kamiya, M.2    Takahara, T.3    Maeda, T.4
  • 92
    • 81855183664 scopus 로고    scopus 로고
    • TORC1 regulates endocytosis via npr1-mediated phosphoinhibition of a ubiquitin ligase adaptor
    • 2-s2.0-81855183664 10.1016/j.cell.2011.09.054
    • MacGurn J. A., Hsu P.-C., Smolka M. B., Emr S. D., TORC1 regulates endocytosis via npr1-mediated phosphoinhibition of a ubiquitin ligase adaptor. Cell 2011 147 5 1104 1117 2-s2.0-81855183664 10.1016/j.cell.2011.09.054
    • (2011) Cell , vol.147 , Issue.5 , pp. 1104-1117
    • MacGurn, J.A.1    Hsu, P.-C.2    Smolka, M.B.3    Emr, S.D.4
  • 93
    • 77958046490 scopus 로고    scopus 로고
    • α -arrestins Aly1 and Aly2 regulate intracellular trafficking in response to nutrient signaling
    • 2-s2.0-77958046490 10.1091/mbc.E10-07-0636
    • O'Donnell A. F., Apffel A., Gardner R. G., Cyert M. S., α -arrestins Aly1 and Aly2 regulate intracellular trafficking in response to nutrient signaling. Molecular Biology of the Cell 2010 21 20 3552 3566 2-s2.0-77958046490 10.1091/mbc.E10-07-0636
    • (2010) Molecular Biology of the Cell , vol.21 , Issue.20 , pp. 3552-3566
    • O'Donnell, A.F.1    Apffel, A.2    Gardner, R.G.3    Cyert, M.S.4
  • 94
    • 84858230240 scopus 로고    scopus 로고
    • Formation and release of arrestin domain-containing protein 1-mediated microvesicles (ARMMs) at plasma membrane by recruitment of TSG101 protein
    • 2-s2.0-84858230240 10.1073/pnas.1200448109
    • Nabhan J. F., Hu R., Oh R. S., Cohen S. N., Lu Q., Formation and release of arrestin domain-containing protein 1-mediated microvesicles (ARMMs) at plasma membrane by recruitment of TSG101 protein. Proceedings of the National Academy of Sciences of the United States of America 2012 109 11 4146 4151 2-s2.0-84858230240 10.1073/pnas.1200448109
    • (2012) Proceedings of the National Academy of Sciences of the United States of America , vol.109 , Issue.11 , pp. 4146-4151
    • Nabhan, J.F.1    Hu, R.2    Oh, R.S.3    Cohen, S.N.4    Lu, Q.5
  • 95
    • 77955058247 scopus 로고    scopus 로고
    • 2-adrenergic receptor
    • 2-s2.0-77955058247 10.1038/embor.2010.80
    • 2-adrenergic receptor. EMBO Reports 2010 11 8 605 611 2-s2.0-77955058247 10.1038/embor.2010.80
    • (2010) EMBO Reports , vol.11 , Issue.8 , pp. 605-611
    • Nabhan, J.F.1    Pan, H.2    Lu, Q.3
  • 96
    • 79952588626 scopus 로고    scopus 로고
    • Multiple interactions between the ESCRT machinery and arrestin-related proteins: Implications for PPXY-dependent budding
    • 2-s2.0-79952588626 10.1128/JVI.02045-10
    • Rauch S., Martin-Serrano J., Multiple interactions between the ESCRT machinery and arrestin-related proteins: implications for PPXY-dependent budding. Journal of Virology 2011 85 7 3546 3556 2-s2.0-79952588626 10.1128/JVI.02045-10
    • (2011) Journal of Virology , vol.85 , Issue.7 , pp. 3546-3556
    • Rauch, S.1    Martin-Serrano, J.2
  • 97
    • 77950580572 scopus 로고    scopus 로고
    • The ubiquitin ligase itch regulates apoptosis by targeting thioredoxin-interacting protein for ubiquitin-dependent degradation
    • 2-s2.0-77950580572 10.1074/jbc.M109.063321
    • Zhang P., Wang C., Gao K., Wang D., Mao J., An J., Xu C., Wu D., Yu H., Liu J. O., Yu L., The ubiquitin ligase itch regulates apoptosis by targeting thioredoxin-interacting protein for ubiquitin-dependent degradation. Journal of Biological Chemistry 2010 285 12 8869 8879 2-s2.0-77950580572 10.1074/jbc.M109.063321
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.12 , pp. 8869-8879
    • Zhang, P.1    Wang, C.2    Gao, K.3    Wang, D.4    Mao, J.5    An, J.6    Xu, C.7    Wu, D.8    Yu, H.9    Liu, J.O.10    Yu, L.11
  • 99
    • 77956643654 scopus 로고    scopus 로고
    • ARRDC3 suppresses breast cancer progression by negatively regulating integrin β 4
    • 2-s2.0-77956643654 10.1038/onc.2010.250
    • Draheim K. M., Chen H. B., Tao Q., Moore N., Roche M., Lyle S., ARRDC3 suppresses breast cancer progression by negatively regulating integrin β 4. Oncogene 2010 29 36 5032 5047 2-s2.0-77956643654 10.1038/onc.2010.250
    • (2010) Oncogene , vol.29 , Issue.36 , pp. 5032-5047
    • Draheim, K.M.1    Chen, H.B.2    Tao, Q.3    Moore, N.4    Roche, M.5    Lyle, S.6
  • 100
    • 44949242315 scopus 로고    scopus 로고
    • Ambient pH gene regulation in fungi: Making connections
    • 2-s2.0-44949242315 10.1016/j.tim.2008.03.006
    • Pealva M. A., Tilburn J., Bignell E., Arst H. N. Jr., Ambient pH gene regulation in fungi: making connections. Trends in Microbiology 2008 16 6 291 300 2-s2.0-44949242315 10.1016/j.tim.2008.03.006
    • (2008) Trends in Microbiology , vol.16 , Issue.6 , pp. 291-300
    • Pealva, M.A.1    Tilburn, J.2    Bignell, E.3    Arst, Jr.H.N.4
  • 101
    • 27144493736 scopus 로고    scopus 로고
    • Constitutive activation of the pH-responsive Rim101 pathway in yeast mutants defective in late steps of the MVB/ESCRT pathway
    • DOI 10.1128/MCB.25.21.9478-9490.2005
    • Hayashi M., Fukuzawa T., Sorimachi H., Maeda T., Constitutive activation of the pH-responsive Rim101 pathway in yeast mutants defective in late steps of the MVB/ESCRT pathway. Molecular and Cellular Biology 2005 25 21 9478 9490 2-s2.0-27144493736 10.1128/MCB.25.21.9478-9490.2005 (Pubitemid 41507848)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.21 , pp. 9478-9490
    • Hayashi, M.1    Fukuzawa, T.2    Sorimachi, H.3    Maeda, T.4
  • 102
    • 9444284398 scopus 로고    scopus 로고
    • Multivesicular body-ESCRT components function in pH response regulation in Saccharomyces cerevisiae and Candida albicans
    • DOI 10.1091/mbc.E04-08-0666
    • Xu W., Smith F. J. Jr., Subaran R., Mitchell A. P., Multivesicular body-ESCRT components function in pH response regulation in Saccharomyces cerevisiae and Candida albicans. Molecular Biology of the Cell 2004 15 12 5528 5537 2-s2.0-9444284398 10.1091/mbc.E04-08-0666 (Pubitemid 39564744)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.12 , pp. 5528-5537
    • Xu, W.1    Smith Jr., F.J.2    Subaran, R.3    Mitchell, A.P.4
  • 103
    • 33644849463 scopus 로고    scopus 로고
    • Control of Bro1-domain protein Rim20 localization by external pH, ESCRT machinery, and the Saccharomyces cerevisiae Rim101 pathway
    • DOI 10.1091/mbc.E05-10-0949
    • Boysen J. H., Mitchell A. P., Control of Bro1-domain protein Rim20 localization by external pH, ESCRT machinery, and the Saccharomyces cerevisiae Rim101 pathway. Molecular Biology of the Cell 2006 17 3 1344 1353 2-s2.0-33644849463 10.1091/mbc.E05-10-0949 (Pubitemid 43376554)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.3 , pp. 1344-1353
    • Boysen, J.H.1    Mitchell, A.P.2
  • 104
    • 84860352444 scopus 로고    scopus 로고
    • An ordered pathway for the assembly of fungal ESCRT-containing ambient pH signalling complexes at the plasma membrane
    • 2-s2.0-84860352444 10.1242/jcs.098897
    • Galindo A., Calcagno-Pizarelli A. M., Arst H. N. Jr., Pealva M. Á., An ordered pathway for the assembly of fungal ESCRT-containing ambient pH signalling complexes at the plasma membrane. Journal of Cell Science 2012 125 7 1784 1795 2-s2.0-84860352444 10.1242/jcs.098897
    • (2012) Journal of Cell Science , vol.125 , Issue.7 , pp. 1784-1795
    • Galindo, A.1    Calcagno-Pizarelli, A.M.2    Arst, Jr.H.N.3    Pealva, M.Á.4
  • 106
    • 84859593755 scopus 로고    scopus 로고
    • Differential requirements of mammalian ESCRTs in multivesicular body formation, virus budding and cell division
    • 2-s2.0-84859593755 10.1111/j.1742-4658.2012.08534.x
    • Morita E., Differential requirements of mammalian ESCRTs in multivesicular body formation, virus budding and cell division. The FEBS Journal 2012 279 8 1399 1406 2-s2.0-84859593755 10.1111/j.1742-4658.2012.08534.x
    • (2012) The FEBS Journal , vol.279 , Issue.8 , pp. 1399-1406
    • Morita, E.1
  • 107
    • 35748944113 scopus 로고    scopus 로고
    • Ubiquitination of β-arrestin links seven-transmembrane receptor endocytosis and ERK activation
    • DOI 10.1074/jbc.M700852200
    • Shenoy S. K., Barak L. S., Xiao K., Ahn S., Berthouze M., Shukla A. K., Luttrell L. M., Lefkowitz R. J., Ubiquitination of β -arrestin links seven-transmembrane receptor endocytosis and ERK activation. Journal of Biological Chemistry 2007 282 40 29549 29562 2-s2.0-35748944113 10.1074/jbc.M700852200 (Pubitemid 350043390)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.40 , pp. 29549-29562
    • Shenoy, S.K.1    Barak, L.S.2    Xiao, K.3    Ahn, S.4    Berthouze, M.5    Shukla, A.K.6    Luttrell, L.M.7    Lefkowitz, R.J.8
  • 108
    • 0034595860 scopus 로고    scopus 로고
    • Differential affinities of visual arrestin, βarrestin1, and βarrestin2 for G protein-coupled receptors delineate two major classes of receptors
    • DOI 10.1074/jbc.M910348199
    • Oakley R. H., Laporte S. A., Holt J. A., Caron M. G., Barak L. S., Differential affinities of visual arrestin, β arrestin1, and β arrestin2 for G protein-coupled receptors delineate two major classes of receptors. Journal of Biological Chemistry 2000 275 22 17201 17210 2-s2.0-0034595860 10.1074/jbc.M910348199 (Pubitemid 30398969)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.22 , pp. 17201-17210
    • Oakley, R.H.1    Laporte, S.A.2    Holt, J.A.3    Caron, M.G.4    Barak, L.S.5
  • 109
    • 33845870964 scopus 로고    scopus 로고
    • Arrestins: Ubiquitous regulators of cellular signaling pathways
    • DOI 10.1186/gb-2006-7-9-236
    • Gurevich E. V., Gurevich V. V., Arrestins: ubiquitous regulators of cellular signaling pathways. Genome Biology 2006 7 9, article 236 2-s2.0-33845870964 10.1186/gb-2006-7-9-236 (Pubitemid 46024028)
    • (2006) Genome Biology , vol.7 , Issue.9 , pp. 236
    • Gurevich, E.V.1    Gurevich, V.V.2
  • 110
    • 77952913696 scopus 로고    scopus 로고
    • Receptor-independent ambient pH signaling by ubiquitin attachment to fungal arrestin-like PalF
    • 2-s2.0-77952913696 10.1074/jbc.M110.114371
    • Hervás-Aguilar A., Galindo A., Pealva M. A., Receptor-independent ambient pH signaling by ubiquitin attachment to fungal arrestin-like PalF. Journal of Biological Chemistry 2010 285 23 18095 18102 2-s2.0-77952913696 10.1074/jbc.M110.114371
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.23 , pp. 18095-18102
    • Hervás-Aguilar, A.1    Galindo, A.2    Pealva, M.A.3
  • 111
    • 36749010218 scopus 로고    scopus 로고
    • The Age of Crosstalk: Phosphorylation, Ubiquitination, and Beyond
    • DOI 10.1016/j.molcel.2007.11.019, PII S1097276507007988
    • Hunter T., The age of crosstalk: phosphorylation, ubiquitination, and beyond. Molecular Cell 2007 28 5 730 738 2-s2.0-36749010218 10.1016/j.molcel. 2007.11.019 (Pubitemid 350217067)
    • (2007) Molecular Cell , vol.28 , Issue.5 , pp. 730-738
    • Hunter, T.1
  • 112
    • 0030680131 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis of the β-adrenergic receptor is regulated by phosphorylation/dephosphorylation of β-arrestin1
    • DOI 10.1074/jbc.272.49.31051
    • Lin F. T., Krueger K. M., Kendall H. E., Daaka Y., Fredericks Z. L., Pitcher J. A., Lefkowitz R. J., Clathrin-mediated endocytosis of the β -adrenergic receptor is regulated by phosphorylation/dephosphorylation of β -arrestin1. Journal of Biological Chemistry 1997 272 49 31051 31057 2-s2.0-0030680131 10.1074/jbc.272.49.31051 (Pubitemid 27527552)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.49 , pp. 31051-31057
    • Lin, F.-T.1    Krueger, K.M.2    Kendall, H.E.3    Daaka, Y.4    Fredericks, Z.L.5    Pitcher, J.A.6    Lefkowitz, R.J.7
  • 114
    • 0033638395 scopus 로고    scopus 로고
    • A molecular pathway for light-dependent photoreceptor apoptosis in Drosophila
    • 2-s2.0-0033638395
    • Kiselev A., Socolich M., Vinos J., Hardy R. W., Zuker C. S., Ranganathan R., A molecular pathway for light-dependent photoreceptor apoptosis in Drosophila. Neuron 2000 28 1 139 152 2-s2.0-0033638395
    • (2000) Neuron , vol.28 , Issue.1 , pp. 139-152
    • Kiselev, A.1    Socolich, M.2    Vinos, J.3    Hardy, R.W.4    Zuker, C.S.5    Ranganathan, R.6
  • 115
    • 0033522896 scopus 로고    scopus 로고
    • Feedback regulation of β-arrestin1 function by extracellular signal- regulated kinases
    • DOI 10.1074/jbc.274.23.15971
    • Lin F. T., Miller W. E., Luttrell L. M., Lefkowitz R. J., Feedback regulation of β -arrestin1 function by extracellular signal- regulated kinases. Journal of Biological Chemistry 1999 274 23 15971 15974 2-s2.0-0033522896 10.1074/jbc.274.23.15971 (Pubitemid 29269294)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.23 , pp. 15971-15974
    • Lin, F.-T.1    Miller, W.E.2    Luttrell, L.M.3    Lefkowitz, R.J.4
  • 116
    • 84860332365 scopus 로고    scopus 로고
    • The β -arrestin-like protein Rim8 is hyperphosphorylated and complexes with Rim21 and Rim101 to promote adaptation to neutral-alkaline pH
    • 2-s2.0-84860332365 10.1128/EC.05211-11
    • Gomez-Raja J., Davis D. A., The β -arrestin-like protein Rim8 is hyperphosphorylated and complexes with Rim21 and Rim101 to promote adaptation to neutral-alkaline pH. Eukaryotic Cell 2012 11 5 683 693 2-s2.0-84860332365 10.1128/EC.05211-11
    • (2012) Eukaryotic Cell , vol.11 , Issue.5 , pp. 683-693
    • Gomez-Raja, J.1    Davis, D.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.