메뉴 건너뛰기




Volumn 126, Issue 16, 2013, Pages 3770-3781

Reciprocal cross-regulation between RNF41 and USP8 controls cytokine receptor sorting and processing

Author keywords

Cathepsin L cleavage; Ectodomain shedding; Nrdp1; RNF41; Type 1 cytokine receptor; USP8

Indexed keywords

CATHEPSIN L; CYTOKINE RECEPTOR; ESCRT PROTEIN; LEPTIN; LEUKEMIA INHIBITORY FACTOR RECEPTOR; LEUKEMIA INHIBITORY FACTOR RECEPTOR ALPHA; PROTEINASE; RING FINGER PROTEIN; RING FINGER PROTEIN 41; UBIQUITIN SPECIFIC PROTEASE 8; UNCLASSIFIED DRUG;

EID: 84883423019     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.131250     Document Type: Article
Times cited : (43)

References (68)
  • 1
    • 33847254975 scopus 로고    scopus 로고
    • UBPY-mediated epidermal growth factor receptor (EGFR) de-ubiquitination promotes EGFR degradation.
    • Alwan, H. A. J. and van Leeuwen, J. E. M. (2007). UBPY-mediated epidermal growth factor receptor (EGFR) de-ubiquitination promotes EGFR degradation. J. Biol. Chem. 282, 1658-1669.
    • (2007) J. Biol. Chem. , vol.282 , pp. 1658-1669
    • Alwan, H.A.J.1    van Leeuwen, J.E.M.2
  • 2
    • 79955414007 scopus 로고    scopus 로고
    • Hrs recognizes a hydrophobic amino acid cluster in cytokine receptors during ubiquitin-independent endosomal sorting.
    • Amano, Y., Yamashita, Y., Kojima, K., Yoshino, K., Tanaka, N., Sugamura, K. and Takeshita, T. (2011). Hrs recognizes a hydrophobic amino acid cluster in cytokine receptors during ubiquitin-independent endosomal sorting. J. Biol. Chem. 286, 15458-15472.
    • (2011) J. Biol. Chem. , vol.286 , pp. 15458-15472
    • Amano, Y.1    Yamashita, Y.2    Kojima, K.3    Yoshino, K.4    Tanaka, N.5    Sugamura, K.6    Takeshita, T.7
  • 3
    • 33846021632 scopus 로고    scopus 로고
    • Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8).
    • Avvakumov, G. V., Walker, J. R., Xue, S., Finerty, P. J., Jr, Mackenzie, F., Newman, E. M. and Dhe-Paganon, S. (2006). Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8). J. Biol. Chem. 281, 38061-38070.
    • (2006) J. Biol. Chem. , vol.281 , pp. 38061-38070
    • Avvakumov, G.V.1    Walker, J.R.2    Xue, S.3    Finerty, P.J.4    Mackenzie, F.5    Newman, E.M.6    Dhe-Paganon, S.7
  • 4
    • 80355148474 scopus 로고    scopus 로고
    • Role of ubiquitylation and USP8-dependent deubiquitylation in the endocytosis and lysosomal targeting of plasma membrane KCa3.1
    • Balut, C. M., Loch, C. M. and Devor, D. C. (2011). Role of ubiquitylation and USP8-dependent deubiquitylation in the endocytosis and lysosomal targeting of plasma membrane KCa3.1. FASEB J. 25, 3938-3948.
    • (2011) FASEB J , vol.25 , pp. 3938-3948
    • Balut, C.M.1    Loch, C.M.2    Devor, D.C.3
  • 5
    • 33644864967 scopus 로고    scopus 로고
    • Ubiquitylation of leptin receptor OB-Ra regulates its clathrin-mediated endocytosis.
    • Belouzard, S. and Rouillé, Y. (2006). Ubiquitylation of leptin receptor OB-Ra regulates its clathrin-mediated endocytosis. EMBO J. 25, 932-942.
    • (2006) EMBO J. , vol.25 , pp. 932-942
    • Belouzard, S.1    Rouillé, Y.2
  • 6
    • 3142546889 scopus 로고    scopus 로고
    • Low levels of expression of leptin receptor at the cell surface result from constitutive endocytosis and intracellular retention in the biosynthetic pathway.
    • Belouzard, S., Delcroix, D. and Rouillé, Y. (2004). Low levels of expression of leptin receptor at the cell surface result from constitutive endocytosis and intracellular retention in the biosynthetic pathway. J. Biol. Chem. 279, 28499-28508.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28499-28508
    • Belouzard, S.1    Delcroix, D.2    Rouillé, Y.3
  • 7
    • 78049404751 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor ubiquitination and trafficking by the USP8·STAM complex.
    • Berlin, I., Schwartz, H. and Nash, P. D. (2010a). Regulation of epidermal growth factor receptor ubiquitination and trafficking by the USP8·STAM complex. J. Biol. Chem. 285, 34909-34921.
    • (2010) J. Biol. Chem. , vol.285 , pp. 34909-34921
    • Berlin, I.1    Schwartz, H.2    Nash, P.D.3
  • 8
    • 78549264851 scopus 로고    scopus 로고
    • The deubiquitinating enzyme USP8 promotes trafficking and degradation of the chemokine receptor 4 at the sorting endosome.
    • Berlin, I., Higginbotham, K. M., Dise, R. S., Sierra, M. I. and Nash, P. D. (2010b). The deubiquitinating enzyme USP8 promotes trafficking and degradation of the chemokine receptor 4 at the sorting endosome. J. Biol. Chem. 285, 37895-37908.
    • (2010) J. Biol. Chem. , vol.285 , pp. 37895-37908
    • Berlin, I.1    Higginbotham, K.M.2    Dise, R.S.3    Sierra, M.I.4    Nash, P.D.5
  • 9
    • 33646171781 scopus 로고    scopus 로고
    • Degradation of endocytosed epidermal growth factor and virally ubiquitinated major histocompatibility complex class I is independent of mammalian ESCRTII.
    • Bowers, K., Piper, S. C., Edeling, M. A., Gray, S. R., Owen, D. J., Lehner, P. J. and Luzio, J. P. (2006). Degradation of endocytosed epidermal growth factor and virally ubiquitinated major histocompatibility complex class I is independent of mammalian ESCRTII. J. Biol. Chem. 281, 5094-5105.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5094-5105
    • Bowers, K.1    Piper, S.C.2    Edeling, M.A.3    Gray, S.R.4    Owen, D.J.5    Lehner, P.J.6    Luzio, J.P.7
  • 10
    • 33947245587 scopus 로고    scopus 로고
    • Neuregulininduced ErbB3 downregulation is mediated by a protein stability cascade involving the E3 ubiquitin ligase Nrdp1.
    • Cao, Z., Wu, X., Yen, L., Sweeney, C. and Carraway, K. L., 3rd (2007). Neuregulininduced ErbB3 downregulation is mediated by a protein stability cascade involving the E3 ubiquitin ligase Nrdp1. Mol. Cell. Biol. 27, 2180-2188.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 2180-2188
    • Cao, Z.1    Wu, X.2    Yen, L.3    Sweeney, C.4    Carraway, K.L.5
  • 11
    • 77955021116 scopus 로고    scopus 로고
    • Nrdp1-mediated regulation of ErbB3 expression by the androgen receptor in androgen-dependent but not castrate-resistant prostate cancer cells.
    • Chen, L., Siddiqui, S., Bose, S., Mooso, B., Asuncion, A., Bedolla, R. G., Vinall, R., Tepper, C. G., Gandour-Edwards, R., Shi, X. et al. (2010). Nrdp1-mediated regulation of ErbB3 expression by the androgen receptor in androgen-dependent but not castrate-resistant prostate cancer cells. Cancer Res. 70, 5994-6003.
    • (2010) Cancer Res. , vol.70 , pp. 5994-6003
    • Chen, L.1    Siddiqui, S.2    Bose, S.3    Mooso, B.4    Asuncion, A.5    Bedolla, R.G.6    Vinall, R.7    Tepper, C.G.8    Gandour-Edwards, R.9    Shi, X.10
  • 12
    • 84866006042 scopus 로고    scopus 로고
    • Governance of endocytic trafficking and signaling by reversible ubiquitylation.
    • Clague, M. J., Liu, H. and Urbé, S. (2012). Governance of endocytic trafficking and signaling by reversible ubiquitylation. Dev. Cell 23, 457-467.
    • (2012) Dev. Cell , vol.23 , pp. 457-467
    • Clague, M.J.1    Liu, H.2    Urbé, S.3
  • 13
    • 52949090018 scopus 로고    scopus 로고
    • SOCS regulation of the JAK/STAT signalling pathway.
    • Croker, B. A., Kiu, H. and Nicholson, S. E. (2008). SOCS regulation of the JAK/STAT signalling pathway. Semin. Cell Dev. Biol. 19, 414-422.
    • (2008) Semin. Cell Dev. Biol. , vol.19 , pp. 414-422
    • Croker, B.A.1    Kiu, H.2    Nicholson, S.E.3
  • 18
    • 0029585762 scopus 로고
    • Rab 7: an important regulator of late endocytic membrane traffic.
    • Feng, Y., Press, B. and Wandinger-Ness, A. (1995). Rab 7: an important regulator of late endocytic membrane traffic. J. Cell Biol. 131, 1435-1452.
    • (1995) J. Cell Biol. , vol.131 , pp. 1435-1452
    • Feng, Y.1    Press, B.2    Wandinger-Ness, A.3
  • 19
    • 79960381005 scopus 로고    scopus 로고
    • Quantity control of the ErbB3 receptor tyrosine kinase at the endoplasmic reticulum.
    • Fry, W. H. D., Simion, C., Sweeney, C. and Carraway, K. L., 3rd (2011). Quantity control of the ErbB3 receptor tyrosine kinase at the endoplasmic reticulum. Mol. Cell. Biol. 31, 3009-3018.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 3009-3018
    • Fry, W.H.D.1    Simion, C.2    Sweeney, C.3    Carraway, K.L.4
  • 20
    • 22144453890 scopus 로고    scopus 로고
    • Ubiquitination of the common cytokine receptor gammac and regulation of expression by an ubiquitination/deubiquitination machinery.
    • Gesbert, F., Malardé, V. and Dautry-Varsat, A. (2005). Ubiquitination of the common cytokine receptor gammac and regulation of expression by an ubiquitination/deubiquitination machinery. Biochem. Biophys. Res. Commun. 334, 474-480.
    • (2005) Biochem. Biophys. Res. Commun. , vol.334 , pp. 474-480
    • Gesbert, F.1    Malardé, V.2    Dautry-Varsat, A.3
  • 21
    • 70349750269 scopus 로고    scopus 로고
    • Investigating the targets of MIR-15a and MIR-16-1 in patients with chronic lymphocytic leukemia (CLL)
    • Hanlon, K., Rudin, C. E. and Harries, L. W. (2009). Investigating the targets of MIR-15a and MIR-16-1 in patients with chronic lymphocytic leukemia (CLL). PLoS ONE 4, e7169.
    • (2009) PLoS ONE , vol.4 , pp. 7169
    • Hanlon, K.1    Rudin, C.E.2    Harries, L.W.3
  • 22
    • 70350514475 scopus 로고    scopus 로고
    • Endosomal deubiquitinating enzymes control ubiquitination and down-regulation of protease-activated receptor 2.
    • Hasdemir, B., Murphy, J. E., Cottrell, G. S. and Bunnett, N. W. (2009). Endosomal deubiquitinating enzymes control ubiquitination and down-regulation of protease-activated receptor 2. J. Biol. Chem. 284, 28453-28466.
    • (2009) J. Biol. Chem. , vol.284 , pp. 28453-28466
    • Hasdemir, B.1    Murphy, J.E.2    Cottrell, G.S.3    Bunnett, N.W.4
  • 23
    • 67749127754 scopus 로고    scopus 로고
    • Ubiquitination regulates proteolytic processing of G protein-coupled receptors after their sorting to lysosomes.
    • Hislop, J. N., Henry, A. G., Marchese, A. and von Zastrow, M. (2009). Ubiquitination regulates proteolytic processing of G protein-coupled receptors after their sorting to lysosomes. J. Biol. Chem. 284, 19361-19370.
    • (2009) J. Biol. Chem. , vol.284 , pp. 19361-19370
    • Hislop, J.N.1    Henry, A.G.2    Marchese, A.3    von Zastrow, M.4
  • 25
    • 80555140057 scopus 로고    scopus 로고
    • Regulation of interleukin-10 receptor ubiquitination and stability by beta-TrCP-containing ubiquitin E3 ligase
    • Jiang, H., Lu, Y., Yuan, L. and Liu, J. (2011). Regulation of interleukin-10 receptor ubiquitination and stability by beta-TrCP-containing ubiquitin E3 ligase. PLoS ONE 6, e27464.
    • (2011) PLoS ONE , vol.6 , pp. 27464
    • Jiang, H.1    Lu, Y.2    Yuan, L.3    Liu, J.4
  • 26
    • 49349109951 scopus 로고    scopus 로고
    • E3 ligase FLRF (Rnf41) regulates differentiation of hematopoietic progenitors by governing steady-state levels of cytokine and retinoic acid receptors.
    • Jing, X., Infante, J., Nachtman, R. G. and Jurecic, R. (2008). E3 ligase FLRF (Rnf41) regulates differentiation of hematopoietic progenitors by governing steady-state levels of cytokine and retinoic acid receptors. Exp. Hematol. 36, 1110-1120.
    • (2008) Exp. Hematol. , vol.36 , pp. 1110-1120
    • Jing, X.1    Infante, J.2    Nachtman, R.G.3    Jurecic, R.4
  • 27
    • 70350150000 scopus 로고    scopus 로고
    • The emerging complexity of protein ubiquitination.
    • Komander, D. (2009). The emerging complexity of protein ubiquitination. Biochem. Soc. Trans. 37, 937-953.
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 937-953
    • Komander, D.1
  • 31
    • 47249161108 scopus 로고    scopus 로고
    • Molecular mechanisms of soluble cytokine receptor generation.
    • Levine, S. J. (2008). Molecular mechanisms of soluble cytokine receptor generation. J. Biol. Chem. 283, 14177-14181.
    • (2008) J. Biol. Chem. , vol.283 , pp. 14177-14181
    • Levine, S.J.1
  • 32
    • 1942453784 scopus 로고    scopus 로고
    • Negative regulation of prolactin receptor stability and signaling mediated by SCF-TRCP E3 ubiquitin ligase.
    • Li, Y., Kumar, K. G. S., Tang, W., Spiegelman, V. S. and Fuchs, S. Y. (2004). Negative regulation of prolactin receptor stability and signaling mediated by SCF-TRCP E3 ubiquitin ligase. Mol. Cell. Biol. 24, 4038-4048.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4038-4048
    • Li, Y.1    Kumar, K.G.S.2    Tang, W.3    Spiegelman, V.S.4    Fuchs, S.Y.5
  • 34
    • 0034801977 scopus 로고    scopus 로고
    • Generation of human soluble leptin receptor by proteolytic cleavage of membrane-anchored receptors.
    • Maamra, M., Bidlingmaier, M., Postel-Vinay, M.-C., Wu, Z., Strasburger, C. J. and Ross, R. J. M. (2001). Generation of human soluble leptin receptor by proteolytic cleavage of membrane-anchored receptors. Endocrinology 142, 4389-4393.
    • (2001) Endocrinology , vol.142 , pp. 4389-4393
    • Maamra, M.1    Bidlingmaier, M.2    Postel-Vinay, M.-C.3    Wu, Z.4    Strasburger, C.J.5    Ross, R.J.M.6
  • 37
    • 79953220455 scopus 로고    scopus 로고
    • ESCRT-0 assembles as a heterotetrameric complex on membranes and binds multiple ubiquitinylated cargoes simultaneously.
    • Mayers, J. R., Fyfe, I., Schuh, A. L., Chapman, E. R., Edwardson, J. M. and Audhya, A. (2011). ESCRT-0 assembles as a heterotetrameric complex on membranes and binds multiple ubiquitinylated cargoes simultaneously. J. Biol. Chem. 286, 9636-9645.
    • (2011) J. Biol. Chem. , vol.286 , pp. 9636-9645
    • Mayers, J.R.1    Fyfe, I.2    Schuh, A.L.3    Chapman, E.R.4    Edwardson, J.M.5    Audhya, A.6
  • 38
    • 84873323769 scopus 로고    scopus 로고
    • The Usp8 deubiquitination enzyme is post-translationally modified by tyrosine and serine phosphorylation.
    • Meijer, I. M. J., Kerperien, J., Sotoca, A. M., van Zoelen, E. J. J. and van Leeuwen, J. E. M. (2013). The Usp8 deubiquitination enzyme is post-translationally modified by tyrosine and serine phosphorylation. Cell. Signal. 25, 919-930.
    • (2013) Cell. Signal. , vol.25 , pp. 919-930
    • Meijer, I.M.J.1    Kerperien, J.2    Sotoca, A.M.3    van Zoelen, E.J.J.4    van Leeuwen, J.E.M.5
  • 39
    • 34250027624 scopus 로고    scopus 로고
    • beta-Trcp mediates ubiquitination and degradation of the erythropoietin receptor and controls cell proliferation.
    • Meyer, L., Deau, B., Forejtníková, H., Duménil, D., Margottin-Goguet, F., Lacombe, C., Mayeux, P. and Verdier, F. (2007). beta-Trcp mediates ubiquitination and degradation of the erythropoietin receptor and controls cell proliferation. Blood 109, 5215-5222.
    • (2007) Blood , vol.109 , pp. 5215-5222
    • Meyer, L.1    Deau, B.2    Forejtníková, H.3    Duménil, D.4    Margottin-Goguet, F.5    Lacombe, C.6    Mayeux, P.7    Verdier, F.8
  • 40
    • 27644438783 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor down-regulation by UBPY-mediated deubiquitination at endosomes.
    • Mizuno, E., Iura, T., Mukai, A., Yoshimori, T., Kitamura, N. and Komada, M. (2005). Regulation of epidermal growth factor receptor down-regulation by UBPY-mediated deubiquitination at endosomes. Mol. Biol. Cell 16, 5163-5174.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5163-5174
    • Mizuno, E.1    Iura, T.2    Mukai, A.3    Yoshimori, T.4    Kitamura, N.5    Komada, M.6
  • 43
    • 84865599600 scopus 로고    scopus 로고
    • Endosomal crosstalk: meeting points for signaling pathways.
    • Pálfy, M., Reményi, A. and Korcsmáros, T. (2012). Endosomal crosstalk: meeting points for signaling pathways. Trends Cell Biol. 22, 447-456.
    • (2012) Trends Cell Biol. , vol.22 , pp. 447-456
    • Pálfy, M.1    Reményi, A.2    Korcsmáros, T.3
  • 44
    • 80755132190 scopus 로고    scopus 로고
    • Endosomal transport via ubiquitination.
    • Piper, R. C. and Lehner, P. J. (2011). Endosomal transport via ubiquitination. Trends Cell Biol. 21, 647-655.
    • (2011) Trends Cell Biol. , vol.21 , pp. 647-655
    • Piper, R.C.1    Lehner, P.J.2
  • 45
    • 0037069388 scopus 로고    scopus 로고
    • Nrdp1/FLRF is a ubiquitin ligase promoting ubiquitination and degradation of the epidermal growth factor receptor family member, ErbB3.
    • Qiu, X.-B. and Goldberg, A. L. (2002). Nrdp1/FLRF is a ubiquitin ligase promoting ubiquitination and degradation of the epidermal growth factor receptor family member, ErbB3. Proc. Natl. Acad. Sci. USA 99, 14843-14848.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14843-14848
    • Qiu, X.-B.1    Goldberg, A.L.2
  • 46
    • 1842457755 scopus 로고    scopus 로고
    • Nrdp1-mediated degradation of the gigantic IAP, BRUCE, is a novel pathway for triggering apoptosis.
    • Qiu, X.-B., Markant, S. L., Yuan, J. and Goldberg, A. L. (2004). Nrdp1-mediated degradation of the gigantic IAP, BRUCE, is a novel pathway for triggering apoptosis. EMBO J. 23, 800-810.
    • (2004) EMBO J. , vol.23 , pp. 800-810
    • Qiu, X.-B.1    Markant, S.L.2    Yuan, J.3    Goldberg, A.L.4
  • 47
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins.
    • Raiborg, C. and Stenmark, H. (2009). The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature 458, 445-452.
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 48
    • 0034941051 scopus 로고    scopus 로고
    • FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes.
    • Raiborg, C., Bremnes, B., Mehlum, A., Gillooly, D. J., D'Arrigo, A., Stang, E. and Stenmark, H. (2001). FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes. J. Cell Sci. 114, 2255-2263.
    • (2001) J. Cell Sci. , vol.114 , pp. 2255-2263
    • Raiborg, C.1    Bremnes, B.2    Mehlum, A.3    Gillooly, D.J.4    D'Arrigo, A.5    Stang, E.6    Stenmark, H.7
  • 49
    • 0032568657 scopus 로고    scopus 로고
    • Hydrolysis of GTP on rab11 is required for the direct delivery of transferrin from the pericentriolar recycling compartment to the cell surface but not from sorting endosomes.
    • Ren, M., Xu, G., Zeng, J., De Lemos-Chiarandini, C., Adesnik, M. and Sabatini, D. D. (1998). Hydrolysis of GTP on rab11 is required for the direct delivery of transferrin from the pericentriolar recycling compartment to the cell surface but not from sorting endosomes. Proc. Natl. Acad. Sci. USA 95, 6187-6192.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6187-6192
    • Ren, M.1    Xu, G.2    Zeng, J.3    De Lemos-Chiarandini, C.4    Adesnik, M.5    Sabatini, D.D.6
  • 50
    • 33646788800 scopus 로고    scopus 로고
    • The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation.
    • Row, P. E., Prior, I. A., McCullough, J., Clague, M. J. and Urbé, S. (2006). The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation. J. Biol. Chem. 281, 12618-12624.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12618-12624
    • Row, P.E.1    Prior, I.A.2    McCullough, J.3    Clague, M.J.4    Urbé, S.5
  • 51
    • 35648973707 scopus 로고    scopus 로고
    • The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation.
    • Row, P. E., Liu, H., Hayes, S., Welchman, R., Charalabous, P., Hofmann, K., Clague, M. J., Sanderson, C. M. and Urbé, S. (2007). The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation. J. Biol. Chem. 282, 30929-30937.
    • (2007) J. Biol. Chem. , vol.282 , pp. 30929-30937
    • Row, P.E.1    Liu, H.2    Hayes, S.3    Welchman, R.4    Charalabous, P.5    Hofmann, K.6    Clague, M.J.7    Sanderson, C.M.8    Urbé, S.9
  • 52
    • 23444461182 scopus 로고    scopus 로고
    • Regulation of gene-activation pathways by PIAS proteins in the immune system.
    • Shuai, K. and Liu, B. (2005). Regulation of gene-activation pathways by PIAS proteins in the immune system. Nat. Rev. Immunol. 5, 593-605.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 593-605
    • Shuai, K.1    Liu, B.2
  • 54
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffic.
    • Stenmark, H. (2009). Rab GTPases as coordinators of vesicle traffic. Nat. Rev. Mol. Cell Biol. 10, 513-525.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 56
    • 17044444647 scopus 로고    scopus 로고
    • STAM, signal transducing adaptor molecule, is associated with Janus kinases and involved in signaling for cell growth and c-myc induction.
    • Takeshita, T., Arita, T., Higuchi, M., Asao, H., Endo, K., Kuroda, H., Tanaka, N., Murata, K., Ishii, N. and Sugamura, K. (1997). STAM, signal transducing adaptor molecule, is associated with Janus kinases and involved in signaling for cell growth and c-myc induction. Immunity 6, 449-457.
    • (1997) Immunity , vol.6 , pp. 449-457
    • Takeshita, T.1    Arita, T.2    Higuchi, M.3    Asao, H.4    Endo, K.5    Kuroda, H.6    Tanaka, N.7    Murata, K.8    Ishii, N.9    Sugamura, K.10
  • 58
    • 84863012484 scopus 로고    scopus 로고
    • Identification of molecular vulnerabilities in human multiple myeloma cells by RNA interference lethality screening of the druggable genome.
    • Tiedemann, R. E., Zhu, Y. X., Schmidt, J., Shi, C. X., Sereduk, C., Yin, H., Mousses, S. and Stewart, A. K. (2012). Identification of molecular vulnerabilities in human multiple myeloma cells by RNA interference lethality screening of the druggable genome. Cancer Res. 72, 757-768.
    • (2012) Cancer Res. , vol.72 , pp. 757-768
    • Tiedemann, R.E.1    Zhu, Y.X.2    Schmidt, J.3    Shi, C.X.4    Sereduk, C.5    Yin, H.6    Mousses, S.7    Stewart, A.K.8
  • 59
    • 0034007126 scopus 로고    scopus 로고
    • Structural and functional studies on the leukemia inhibitory factor receptor (LIF-R): gene and soluble form of LIF-R, and cytoplasmic domain of LIF-R required for differentiation and growth arrest of myeloid leukemic cells.
    • Tomida, M. (2000). Structural and functional studies on the leukemia inhibitory factor receptor (LIF-R): gene and soluble form of LIF-R, and cytoplasmic domain of LIF-R required for differentiation and growth arrest of myeloid leukemic cells. Leuk. Lymphoma 37, 517-525.
    • (2000) Leuk. Lymphoma , vol.37 , pp. 517-525
    • Tomida, M.1
  • 60
    • 67649229630 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase Nrdp1 'preferentially' promotes TLR-mediated production of type I interferon.
    • Wang, C., Chen, T., Zhang, J., Yang, M., Li, N., Xu, X. and Cao, X. (2009). The E3 ubiquitin ligase Nrdp1 'preferentially' promotes TLR-mediated production of type I interferon. Nat. Immunol. 10, 744-752.
    • (2009) Nat. Immunol. , vol.10 , pp. 744-752
    • Wang, C.1    Chen, T.2    Zhang, J.3    Yang, M.4    Li, N.5    Xu, X.6    Cao, X.7
  • 61
    • 79952811396 scopus 로고    scopus 로고
    • RNF41 (Nrdp1) controls type 1 cytokine receptor degradation and ectodomain shedding.
    • Wauman, J., De Ceuninck, L., Vanderroost, N., Lievens, S. and Tavernier, J. (2011). RNF41 (Nrdp1) controls type 1 cytokine receptor degradation and ectodomain shedding. J. Cell Sci. 124, 921-932.
    • (2011) J. Cell Sci. , vol.124 , pp. 921-932
    • Wauman, J.1    De Ceuninck, L.2    Vanderroost, N.3    Lievens, S.4    Tavernier, J.5
  • 62
    • 67649888820 scopus 로고    scopus 로고
    • Site-specific ubiquitination determines lysosomal sorting and signal attenuation of the granulocyte colony-stimulating factor receptor.
    • Wölfler, A., Irandoust, M., Meenhuis, A., Gits, J., Roovers, O. and Touw, I. P. (2009). Site-specific ubiquitination determines lysosomal sorting and signal attenuation of the granulocyte colony-stimulating factor receptor. Traffic 10, 1168-1179.
    • (2009) Traffic , vol.10 , pp. 1168-1179
    • Wölfler, A.1    Irandoust, M.2    Meenhuis, A.3    Gits, J.4    Roovers, O.5    Touw, I.P.6
  • 63
    • 79955940965 scopus 로고    scopus 로고
    • Regulation of endocytic sorting by ESCRT-DUB-mediated deubiquitination.
    • Wright, M. H., Berlin, I. and Nash, P. D. (2011). Regulation of endocytic sorting by ESCRT-DUB-mediated deubiquitination. Cell Biochem. Biophys. 60, 39-46.
    • (2011) Cell Biochem. Biophys. , vol.60 , pp. 39-46
    • Wright, M.H.1    Berlin, I.2    Nash, P.D.3
  • 64
    • 4344646977 scopus 로고    scopus 로고
    • Stabilization of the E3 ubiquitin ligase Nrdp1 by the deubiquitinating enzyme USP8
    • Wu, X., Yen, L., Irwin, L., Sweeney, C. and Carraway, K. L., 3rd (2004). Stabilization of the E3 ubiquitin ligase Nrdp1 by the deubiquitinating enzyme USP8. Mol. Cell. Biol. 24, 7748-7757.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 7748-7757
    • Wu, X.1    Yen, L.2    Irwin, L.3    Sweeney, C.4    Carraway, K.L.5
  • 65
    • 42649118836 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in the JAK/STAT pathway.
    • Xu, D. and Qu, C.-K. (2008). Protein tyrosine phosphatases in the JAK/STAT pathway. Frontiers in bioscience 13, 4925-4932.
    • (2008) Frontiers in bioscience , vol.13 , pp. 4925-4932
    • Xu, D.1    Qu, C.-K.2
  • 68
    • 45049084568 scopus 로고    scopus 로고
    • Parkin is ubiquitinated by Nrdp1 and abrogates Nrdp1-induced oxidative stress.
    • Yu, F. and Zhou, J. (2008). Parkin is ubiquitinated by Nrdp1 and abrogates Nrdp1-induced oxidative stress. Neurosci. Lett. 440, 4-8.
    • (2008) Neurosci. Lett. , vol.440 , pp. 4-8
    • Yu, F.1    Zhou, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.