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Volumn 6, Issue MAR, 2015, Pages

Role of E2-Ub-conjugating enzymes during skeletal muscle atrophy

Author keywords

Atrophy; E2 ubiquitin conjugating enzyme; E3 ubiquitin ligase; Proteasome; Skeletal muscle; Ubiquitin

Indexed keywords

ALPHA LACTALBUMIN; ATROGIN 1; INSULIN; MESSENGER RNA; MUSCLE PROTEIN; MUSCLE RING FINGER 1 PROTEIN; PROTEIN MDM2; REACTIVE OXYGEN METABOLITE; RING FINGER PROTEIN; SOMATOMEDIN C; UBIQUITIN CONJUGATING ENZYME 2A; UBIQUITIN CONJUGATING ENZYME 2B; UBIQUITIN CONJUGATING ENZYME 2D; UBIQUITIN CONJUGATING ENZYME 2D2; UBIQUITIN CONJUGATING ENZYME 2E3; UBIQUITIN CONJUGATING ENZYME 2G1; UBIQUITIN CONJUGATING ENZYME 2G2; UBIQUITIN CONJUGATING ENZYME 2J2; UBIQUITIN CONJUGATING ENZYME 2L3; UBIQUITIN CONJUGATING ENZYME 2O; UBIQUITIN CONJUGATING ENZYME E2; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 84926466807     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2015.00059     Document Type: Review
Times cited : (38)

References (123)
  • 1
    • 0036711190 scopus 로고    scopus 로고
    • Ubiquitin-conjugating enzyme E2(14k)/HR6B is dispensable for increased protein catabolism in muscle of fasted mice
    • Adegoke, O. A. J., Bedard, N., Roest, H. P., and Wing, S. S. (2002). Ubiquitin-conjugating enzyme E2(14k)/HR6B is dispensable for increased protein catabolism in muscle of fasted mice. Am. J. Physiol. Endocrinol. Metab . 283, E482-E489. doi: 10.1152/ajpendo.00097.2002
    • (2002) Am. J. Physiol. Endocrinol. Metab. , vol.283 , pp. E482-E489
    • Adegoke, O.A.J.1    Bedard, N.2    Roest, H.P.3    Wing, S.S.4
  • 3
    • 84907606421 scopus 로고    scopus 로고
    • Mulan E3 ubiquitin ligase interacts with multiple E2 conjugating enzymes and participates in mitophagy by recruiting GABARAP
    • Ambivero, C. T., Cilenti, L., Main, S., and Zervos, A. S. (2014). Mulan E3 ubiquitin ligase interacts with multiple E2 conjugating enzymes and participates in mitophagy by recruiting GABARAP. Cell. Signal . 26, 2921-2929. doi: 10.1016/j.cellsig.2014.09.004
    • (2014) Cell. Signal. , vol.26 , pp. 2921-2929
    • Ambivero, C.T.1    Cilenti, L.2    Main, S.3    Zervos, A.S.4
  • 4
    • 76649112438 scopus 로고    scopus 로고
    • UBR2 mediates transcriptional silencing during spermatogenesis via histone ubiquitination
    • An, J. Y., Kim, E. A., Jiang, Y., Zakrzewska, A., Kim, D. E., Lee, M. J., et al. (2010). UBR2 mediates transcriptional silencing during spermatogenesis via histone ubiquitination. Proc. Natl. Acad. Sci. U.S.A . 107, 1912-1917. doi: 10.1073/pnas.0910267107
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 1912-1917
    • An, J.Y.1    Kim, E.A.2    Jiang, Y.3    Zakrzewska, A.4    Kim, D.E.5    Lee, M.J.6
  • 6
    • 0030791425 scopus 로고    scopus 로고
    • Domains required for dimerization of yeast Rad6 ubiquitin-conjugating enzyme and Rad18 DNA binding protein
    • Bailly, V., Prakash, S., and Prakash, L. (1997). Domains required for dimerization of yeast Rad6 ubiquitin-conjugating enzyme and Rad18 DNA binding protein. Mol. Cell. Biol . 17, 4536-4543.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4536-4543
    • Bailly, V.1    Prakash, S.2    Prakash, L.3
  • 7
    • 72949117882 scopus 로고    scopus 로고
    • Gene expression and muscle fiber function in a porcine ICU model
    • Banduseela, V. C., Ochala, J., Chen, Y. W., Goransson, H., Norman, H., Radell, P., et al. (2009). Gene expression and muscle fiber function in a porcine ICU model. Physiol. Genomics 39, 141-159. doi: 10.1152/physiolgenomics.00026.2009
    • (2009) Physiol. Genomics , vol.39 , pp. 141-159
    • Banduseela, V.C.1    Ochala, J.2    Chen, Y.W.3    Goransson, H.4    Norman, H.5    Radell, P.6
  • 8
    • 33846809289 scopus 로고    scopus 로고
    • Atrophy-related ubiquitin ligases atrogin-1 and MuRF-1 are associated with uterine smooth muscle involution in the postpartum period
    • Bdolah, Y., Segal, A., Tanksale, P., Karumanchi, S. A., and Lecker, S. H. (2007). Atrophy-related ubiquitin ligases atrogin-1 and MuRF-1 are associated with uterine smooth muscle involution in the postpartum period. Am. J. Physiol. Regul. Integr. Comp. Physiol . 292, R971-R976. doi: 10.1152/ajpregu.00617.2006
    • (2007) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.292 , pp. R971-R976
    • Bdolah, Y.1    Segal, A.2    Tanksale, P.3    Karumanchi, S.A.4    Lecker, S.H.5
  • 9
    • 0030065766 scopus 로고    scopus 로고
    • Mechanism of ubiquitin conjugating enzyme E2-230K: catalysis involving a thiol relay?
    • Berleth, E. S., and Pickart, C. M. (1996). Mechanism of ubiquitin conjugating enzyme E2-230K: catalysis involving a thiol relay? Biochemistry 35, 1664-1671. doi: 10.1021/bi952105y
    • (1996) Biochemistry , vol.35 , pp. 1664-1671
    • Berleth, E.S.1    Pickart, C.M.2
  • 10
    • 84898754901 scopus 로고    scopus 로고
    • New insights into ubiquitin E3 ligase mechanism
    • Berndsen, C. E., and Wolberger, C. (2014). New insights into ubiquitin E3 ligase mechanism. Nat. Struct. Mol. Biol . 21, 301-307. doi: 10.1038/nsmb.2780
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 301-307
    • Berndsen, C.E.1    Wolberger, C.2
  • 11
    • 84886570071 scopus 로고    scopus 로고
    • Vitamin D deficiency-induced muscle wasting occurs through the ubiquitin proteasome pathway and is partially corrected by calcium in male rats
    • Bhat, M., Kalam, R., Qadri, S. S., Madabushi, S., and Ismail, A. (2013). Vitamin D deficiency-induced muscle wasting occurs through the ubiquitin proteasome pathway and is partially corrected by calcium in male rats. Endocrinology 154, 4018-4029. doi: 10.1210/en.2013-1369
    • (2013) Endocrinology , vol.154 , pp. 4018-4029
    • Bhat, M.1    Kalam, R.2    Qadri, S.S.3    Madabushi, S.4    Ismail, A.5
  • 12
    • 84907727935 scopus 로고    scopus 로고
    • Skeletal muscle atrophy and the E3 ubiquitin ligases MuRF1 and MAFbx/atrogin-1
    • Bodine, S. C., and Baehr, L. M. (2014). Skeletal muscle atrophy and the E3 ubiquitin ligases MuRF1 and MAFbx/atrogin-1. Am. J. Physiol. Endocrinol. Metab . 307, E469-E484. doi: 10.1152/ajpendo.00204.2014
    • (2014) Am. J. Physiol. Endocrinol. Metab. , vol.307 , pp. E469-E484
    • Bodine, S.C.1    Baehr, L.M.2
  • 13
    • 0035941020 scopus 로고    scopus 로고
    • Identification of ubiquitin ligases required for skeletal muscle atrophy
    • Bodine, S. C., Latres, E., Baumhueter, S., Lai, V. K. M., Nunez, L., Clarke, B. A., et al. (2001). Identification of ubiquitin ligases required for skeletal muscle atrophy. Science 294, 1704-1708. doi: 10.1126/science.1065874
    • (2001) Science , vol.294 , pp. 1704-1708
    • Bodine, S.C.1    Latres, E.2    Baumhueter, S.3    Lai, V.K.M.4    Nunez, L.5    Clarke, B.A.6
  • 14
    • 33644850903 scopus 로고    scopus 로고
    • A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination
    • Brzovic, P. S., Lissounov, A., Christensen, D. E., Hoyt, D. W., and Klevit, R. E. (2006). A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination. Mol. Cell 21, 873-880. doi: 10.1016/j.molcel.2006.02.008
    • (2006) Mol. Cell , vol.21 , pp. 873-880
    • Brzovic, P.S.1    Lissounov, A.2    Christensen, D.E.3    Hoyt, D.W.4    Klevit, R.E.5
  • 15
    • 0036768523 scopus 로고    scopus 로고
    • The relationship between skeletal muscle proteolysis and ubiquitin-proteasome proteolytic pathway in burned rats
    • Chai, J., Wu, Y., and Sheng, Z. (2002). The relationship between skeletal muscle proteolysis and ubiquitin-proteasome proteolytic pathway in burned rats. Burns 28, 527-533. doi: 10.1016/S0305-4179(02)00049-9
    • (2002) Burns , vol.28 , pp. 527-533
    • Chai, J.1    Wu, Y.2    Sheng, Z.3
  • 16
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K., et al. (1989). A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 243, 1576-1583. doi: 10.1126/science.2538923
    • (1989) Science , vol.243 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5    Gonda, D.K.6
  • 17
    • 31044437051 scopus 로고    scopus 로고
    • The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site
    • Chen, B., Mariano, J., Tsai, Y. C., Chan, A. H., Cohen, M., and Weissman, A. M. (2006). The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site. Proc. Natl. Acad. Sci. U.S.A . 103, 341-346. doi: 10.1073/pnas.0506618103
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 341-346
    • Chen, B.1    Mariano, J.2    Tsai, Y.C.3    Chan, A.H.4    Cohen, M.5    Weissman, A.M.6
  • 18
    • 84863062108 scopus 로고    scopus 로고
    • RAD6 regulates the dosage of p53 by a combination of transcriptional and posttranscriptional mechanisms
    • Chen, S., Wang, D. L., Liu, Y., Zhao, L., and Sun, F. L. (2012). RAD6 regulates the dosage of p53 by a combination of transcriptional and posttranscriptional mechanisms. Mol. Cell. Biol . 32, 576-587. doi: 10.1128/MCB.05966-11
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 576-587
    • Chen, S.1    Wang, D.L.2    Liu, Y.3    Zhao, L.4    Sun, F.L.5
  • 19
    • 34948848684 scopus 로고    scopus 로고
    • E2-BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages
    • Christensen, D. E., Brzovic, P. S., and Klevit, R. E. (2007). E2-BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages. Nat. Struct. Mol. Biol . 14, 941-948. doi: 10.1038/nsmb1295
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 941-948
    • Christensen, D.E.1    Brzovic, P.S.2    Klevit, R.E.3
  • 20
    • 0033305506 scopus 로고    scopus 로고
    • Regulation of components of the ubiquitin system by insulin-like growth factor I and growth hormone in skeletal muscle of rats made catabolic with dexamethasone
    • Chrysis, D., and Underwood, L. E. (1999). Regulation of components of the ubiquitin system by insulin-like growth factor I and growth hormone in skeletal muscle of rats made catabolic with dexamethasone. Endocrinology 140, 5635-5641. doi: 10.1210/endo.140.12.7217
    • (1999) Endocrinology , vol.140 , pp. 5635-5641
    • Chrysis, D.1    Underwood, L.E.2
  • 21
    • 84890197334 scopus 로고    scopus 로고
    • The complexity of recognition of ubiquitinated substrates by the 26S proteasome
    • Ciechanover, A., and Stanhill, A. (2014). The complexity of recognition of ubiquitinated substrates by the 26S proteasome. Biochim. Biophys. Acta 1843, 86-96. doi: 10.1016/j.bbamcr.2013.07.007
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 86-96
    • Ciechanover, A.1    Stanhill, A.2
  • 22
    • 35548973391 scopus 로고    scopus 로고
    • The E3 Ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle
    • Clarke, B. A., Drujan, D., Willis, M. S., Murphy, L. O., Corpina, R. A., Burova, E., et al. (2007). The E3 Ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle. Cell Metab . 6, 376-385. doi: 10.1016/j.cmet.2007.09.009
    • (2007) Cell Metab. , vol.6 , pp. 376-385
    • Clarke, B.A.1    Drujan, D.2    Willis, M.S.3    Murphy, L.O.4    Corpina, R.A.5    Burova, E.6
  • 23
    • 45749091661 scopus 로고    scopus 로고
    • The CK2 phosphorylation of catalytic domain of Cdc34 modulates its activity at the G1 to S transition in Saccharomyces cerevisiae
    • Coccetti, P., Tripodi, F., Tedeschi, G., Nonnis, S., Marin, O., Fantinato, S., et al. (2008). The CK2 phosphorylation of catalytic domain of Cdc34 modulates its activity at the G1 to S transition in Saccharomyces cerevisiae. Cell Cycle 7, 1391-1401. doi: 10.4161/cc.7.10.5825
    • (2008) Cell Cycle , vol.7 , pp. 1391-1401
    • Coccetti, P.1    Tripodi, F.2    Tedeschi, G.3    Nonnis, S.4    Marin, O.5    Fantinato, S.6
  • 24
    • 67449132363 scopus 로고    scopus 로고
    • During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation
    • Cohen, S., Brault, J. J., Gygi, S. P., Glass, D. J., Valenzuela, D. M., Gartner, C., et al. (2009). During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation. J. Cell. Biol . 185, 1083-1095. doi: 10.1083/jcb.200901052
    • (2009) J. Cell. Biol. , vol.185 , pp. 1083-1095
    • Cohen, S.1    Brault, J.J.2    Gygi, S.P.3    Glass, D.J.4    Valenzuela, D.M.5    Gartner, C.6
  • 25
    • 29244439931 scopus 로고    scopus 로고
    • A leucine-supplemented diet restores the defective postprandial inhibition of proteasome-dependent proteolysis in aged rat skeletal muscle
    • Combaret, L., Dardevet, D., Rieu, I., Pouch, M. N., Bechet, D., Taillandier, D., et al. (2005). A leucine-supplemented diet restores the defective postprandial inhibition of proteasome-dependent proteolysis in aged rat skeletal muscle. J. Physiol . 569, 489-499. doi: 10.1113/jphysiol.2005.098004
    • (2005) J. Physiol. , vol.569 , pp. 489-499
    • Combaret, L.1    Dardevet, D.2    Rieu, I.3    Pouch, M.N.4    Bechet, D.5    Taillandier, D.6
  • 26
    • 0037081769 scopus 로고    scopus 로고
    • Torbafylline (HWA 448) inhibits enhanced skeletal muscle ubiquitin-proteasome-dependent proteolysis in cancer and septic rats
    • Combaret, L., Tilignac, T., Claustre, A., Voisin, L., Taillandier, D., Obled, C., et al. (2002). Torbafylline (HWA 448) inhibits enhanced skeletal muscle ubiquitin-proteasome-dependent proteolysis in cancer and septic rats. Biochem. J . 361, 185-192. doi: 10.1042/0264-6021:3610185
    • (2002) Biochem. J. , vol.361 , pp. 185-192
    • Combaret, L.1    Tilignac, T.2    Claustre, A.3    Voisin, L.4    Taillandier, D.5    Obled, C.6
  • 27
    • 0028881695 scopus 로고
    • Sensitivity and protein turnover response to glucocorticoids are different in skeletal muscle from adult and old rats. Lack of regulation of the ubiquitin-proteasome proteolytic pathway in aging
    • Dardevet, D., Sornet, C., Taillandier, D., Savary, I., Attaix, D., and Grizard, J. (1995). Sensitivity and protein turnover response to glucocorticoids are different in skeletal muscle from adult and old rats. Lack of regulation of the ubiquitin-proteasome proteolytic pathway in aging. J. Clin. Invest . 96, 2113-2119. doi: 10.1172/JCI118264
    • (1995) J. Clin. Invest. , vol.96 , pp. 2113-2119
    • Dardevet, D.1    Sornet, C.2    Taillandier, D.3    Savary, I.4    Attaix, D.5    Grizard, J.6
  • 28
    • 84884286514 scopus 로고    scopus 로고
    • Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine
    • Das, R., Liang, Y. H., Mariano, J., Li, J., Huang, T., King, A., et al. (2013). Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine. EMBO J . 32, 2504-2516. doi: 10.1038/emboj.2013.174
    • (2013) EMBO J. , vol.32 , pp. 2504-2516
    • Das, R.1    Liang, Y.H.2    Mariano, J.3    Li, J.4    Huang, T.5    King, A.6
  • 29
    • 67449110736 scopus 로고    scopus 로고
    • Allosteric activation of E2-RING finger-mediated ubiquitylation by a structurally defined specific E2-binding region of gp78
    • Das, R., Mariano, J., Tsai, Y. C., Kalathur, R. C., Kostova, Z., Li, J., et al. (2009). Allosteric activation of E2-RING finger-mediated ubiquitylation by a structurally defined specific E2-binding region of gp78. Mol. Cell 34, 674-685. doi: 10.1016/j.molcel.2009.05.010
    • (2009) Mol. Cell , vol.34 , pp. 674-685
    • Das, R.1    Mariano, J.2    Tsai, Y.C.3    Kalathur, R.C.4    Kostova, Z.5    Li, J.6
  • 30
    • 77950579617 scopus 로고    scopus 로고
    • The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines
    • David, Y., Ziv, T., Admon, A., and Navon, A. (2010). The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J. Biol. Chem . 285, 8595-8604. doi: 10.1074/jbc.M109.089003
    • (2010) J. Biol. Chem. , vol.285 , pp. 8595-8604
    • David, Y.1    Ziv, T.2    Admon, A.3    Navon, A.4
  • 31
    • 84866124869 scopus 로고    scopus 로고
    • BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer
    • Dou, H., Buetow, L., Sibbet, G. J., Cameron, K., and Huang, D. T. (2012). BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nat. Struct. Mol. Biol . 19, 876-883. doi: 10.1038/nsmb.2379
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 876-883
    • Dou, H.1    Buetow, L.2    Sibbet, G.J.3    Cameron, K.4    Huang, D.T.5
  • 32
    • 33749506057 scopus 로고    scopus 로고
    • Mms2-Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation
    • Eddins, M. J., Carlile, C. M., Gomez, K. M., Pickart, C. M., and Wolberger, C. (2006). Mms2-Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation. Nat. Struct. Mol. Biol . 13, 915-920. doi: 10.1038/nsmb1148
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 915-920
    • Eddins, M.J.1    Carlile, C.M.2    Gomez, K.M.3    Pickart, C.M.4    Wolberger, C.5
  • 33
    • 0034464615 scopus 로고    scopus 로고
    • Insulin-like growth factor I reduces ubiquitin and ubiquitin-conjugating enzyme gene expression but does not inhibit muscle proteolysis in septic rats
    • Fang, C. H., Li, B. G., Sun, X., and Hasselgren, P. O. (2000). Insulin-like growth factor I reduces ubiquitin and ubiquitin-conjugating enzyme gene expression but does not inhibit muscle proteolysis in septic rats. Endocrinology 141, 2743-2751. doi: 10.1210/endo.141.8.7593
    • (2000) Endocrinology , vol.141 , pp. 2743-2751
    • Fang, C.H.1    Li, B.G.2    Sun, X.3    Hasselgren, P.O.4
  • 34
    • 34848818486 scopus 로고    scopus 로고
    • Myosin accumulation and striated muscle myopathy result from the loss of muscle RING finger 1 and 3
    • Fielitz, J., Kim, M. S., Shelton, J. M., Latif, S., Spencer, J. A., Glass, D. J., et al. (2007). Myosin accumulation and striated muscle myopathy result from the loss of muscle RING finger 1 and 3. J. Clin. Invest . 117, 2486-2495. doi: 10.1172/JCI32827
    • (2007) J. Clin. Invest. , vol.117 , pp. 2486-2495
    • Fielitz, J.1    Kim, M.S.2    Shelton, J.M.3    Latif, S.4    Spencer, J.A.5    Glass, D.J.6
  • 35
    • 0034685026 scopus 로고    scopus 로고
    • The gene expression of ubiquitin ligase E3alpha is upregulated in skeletal muscle during sepsis in rats-potential role of glucocorticoids
    • Fischer, D., Sun, X., Gang, G., Pritts, T., and Hasselgren, P. O. (2000). The gene expression of ubiquitin ligase E3alpha is upregulated in skeletal muscle during sepsis in rats-potential role of glucocorticoids. Biochem. Biophys. Res. Commun . 267, 504-508. doi: 10.1006/bbrc.1999.1987
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 504-508
    • Fischer, D.1    Sun, X.2    Gang, G.3    Pritts, T.4    Hasselgren, P.O.5
  • 36
    • 84863224987 scopus 로고    scopus 로고
    • Upregulation of proteasome activity in muscle RING finger 1-null mice following denervation
    • Gomes, A. V., Waddell, D. S., Siu, R., Stein, M., Dewey, S., Furlow, J. D., et al. (2012). Upregulation of proteasome activity in muscle RING finger 1-null mice following denervation. FASEB J . 26, 2986-2999. doi: 10.1096/fj.12-204495
    • (2012) FASEB J. , vol.26 , pp. 2986-2999
    • Gomes, A.V.1    Waddell, D.S.2    Siu, R.3    Stein, M.4    Dewey, S.5    Furlow, J.D.6
  • 37
    • 0032493365 scopus 로고    scopus 로고
    • Basal and human papillomavirus E6 oncoprotein-induced degradation of Myc proteins by the ubiquitin pathway
    • Gross-Mesilaty, S., Reinstein, E., Bercovich, B., Tobias, K. E., Schwartz, A. L., Kahana, C., et al. (1998). Basal and human papillomavirus E6 oncoprotein-induced degradation of Myc proteins by the ubiquitin pathway. Proc. Natl. Acad. Sci. U.S.A . 95, 8058-8063. doi: 10.1073/pnas.95.14.8058
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 8058-8063
    • Gross-Mesilaty, S.1    Reinstein, E.2    Bercovich, B.3    Tobias, K.E.4    Schwartz, A.L.5    Kahana, C.6
  • 38
    • 0028897653 scopus 로고
    • Coordinated induction of the ubiquitin conjugation pathway accompanies the developmentally programmed death of insect skeletal muscle
    • Haas, A. L., Baboshina, O., Williams, B., and Schwartz, L. M. (1995). Coordinated induction of the ubiquitin conjugation pathway accompanies the developmentally programmed death of insect skeletal muscle. J. Biol. Chem . 270, 9407-9412.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9407-9412
    • Haas, A.L.1    Baboshina, O.2    Williams, B.3    Schwartz, L.M.4
  • 39
    • 84874765742 scopus 로고    scopus 로고
    • Regulation of WASH-dependent actin polymerization and protein trafficking by ubiquitination
    • Hao, Y. H., Doyle, J. M., Ramanathan, S., Gomez, T. S., Jia, D., Xu, M., et al. (2013). Regulation of WASH-dependent actin polymerization and protein trafficking by ubiquitination. Cell 152, 1051-1064. doi: 10.1016/j.cell.2013.01.051
    • (2013) Cell , vol.152 , pp. 1051-1064
    • Hao, Y.H.1    Doyle, J.M.2    Ramanathan, S.3    Gomez, T.S.4    Jia, D.5    Xu, M.6
  • 40
    • 48349145549 scopus 로고    scopus 로고
    • Coordinate expression of the 19S regulatory complex and evidence for ubiquitin-dependent telethonin degradation in the unloaded soleus muscle
    • Heng, A. E., Ventadour, S., Jarzaguet, M., Pouch-Pelissier, M. N., Guezennec, C. Y., Bigard, X., et al. (2008). Coordinate expression of the 19S regulatory complex and evidence for ubiquitin-dependent telethonin degradation in the unloaded soleus muscle. Int. J. Biochem. Cell Biol . 40, 2544-2552. doi: 10.1016/j.biocel.2008.04.013
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 2544-2552
    • Heng, A.E.1    Ventadour, S.2    Jarzaguet, M.3    Pouch-Pelissier, M.N.4    Guezennec, C.Y.5    Bigard, X.6
  • 41
    • 79955027304 scopus 로고    scopus 로고
    • E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6
    • Hibbert, R. G., Huang, A., Boelens, R., and Sixma, T. K. (2011). E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. Proc. Natl. Acad. Sci. U.S.A . 108, 5590-5595. doi: 10.1073/pnas.1017516108
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 5590-5595
    • Hibbert, R.G.1    Huang, A.2    Boelens, R.3    Sixma, T.K.4
  • 42
    • 32544444479 scopus 로고    scopus 로고
    • A novel ubiquitin-binding protein ZNF216 functioning in muscle atrophy
    • Hishiya, A., Iemura, S., Natsume, T., Takayama, S., Ikeda, K., and Watanabe, K. (2006). A novel ubiquitin-binding protein ZNF216 functioning in muscle atrophy. EMBO J . 25, 554-564. doi: 10.1038/sj.emboj.7600945
    • (2006) EMBO J. , vol.25 , pp. 554-564
    • Hishiya, A.1    Iemura, S.2    Natsume, T.3    Takayama, S.4    Ikeda, K.5    Watanabe, K.6
  • 43
    • 34250375116 scopus 로고    scopus 로고
    • E3-independent monoubiquitination of ubiquitin-binding proteins
    • Hoeller, D., Hecker, C. M., Wagner, S., Rogov, V., Dotsch, V., and Dikic, I. (2007). E3-independent monoubiquitination of ubiquitin-binding proteins. Mol. Cell 26, 891-898. doi: 10.1016/j.molcel.2007.05.014
    • (2007) Mol. Cell , vol.26 , pp. 891-898
    • Hoeller, D.1    Hecker, C.M.2    Wagner, S.3    Rogov, V.4    Dotsch, V.5    Dikic, I.6
  • 44
    • 0032741446 scopus 로고    scopus 로고
    • Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade
    • Huang, L., Kinnucan, E., Wang, G., Beaudenon, S., Howley, P. M., Huibregtse, J. M., et al. (1999). Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science 286, 1321-1326. doi: 10.1126/science.286.5443.1321
    • (1999) Science , vol.286 , pp. 1321-1326
    • Huang, L.1    Kinnucan, E.2    Wang, G.3    Beaudenon, S.4    Howley, P.M.5    Huibregtse, J.M.6
  • 45
    • 18844465487 scopus 로고    scopus 로고
    • Functional and phylogenetic analysis of the ubiquitylation system in Caenorhabditis elegans: ubiquitin-conjugating enzymes, ubiquitin-activating enzymes, and ubiquitin-like proteins
    • research0002.1-0002.15
    • Jones, D., Crowe, E., Stevens, T. A., and Candido, E. P. (2002). Functional and phylogenetic analysis of the ubiquitylation system in Caenorhabditis elegans: ubiquitin-conjugating enzymes, ubiquitin-activating enzymes, and ubiquitin-like proteins. Genome Biol . 3, research0002.1-0002.15
    • (2002) Genome Biol. , vol.3
    • Jones, D.1    Crowe, E.2    Stevens, T.A.3    Candido, E.P.4
  • 46
    • 77951244767 scopus 로고    scopus 로고
    • Solution structure and dynamics of human ubiquitin conjugating enzyme Ube2g2
    • Ju, T., Bocik, W., Majumdar, A., and Tolman, J. R. (2010). Solution structure and dynamics of human ubiquitin conjugating enzyme Ube2g2. Proteins 78, 1291-1301. doi: 10.1002/prot.22648
    • (2010) Proteins , vol.78 , pp. 1291-1301
    • Ju, T.1    Bocik, W.2    Majumdar, A.3    Tolman, J.R.4
  • 47
    • 11144237310 scopus 로고    scopus 로고
    • Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I
    • Kedar, V., McDonough, H., Arya, R., Li, H. H., Rockman, H. A., and Patterson, C. (2004). Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I. Proc. Natl. Acad. Sci. U.S.A . 101, 18135-18140. doi: 10.1073/pnas.0404341102
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 18135-18140
    • Kedar, V.1    McDonough, H.2    Arya, R.3    Li, H.H.4    Rockman, H.A.5    Patterson, C.6
  • 48
    • 0037319130 scopus 로고    scopus 로고
    • Ubiquitin-proteasome-dependent muscle proteolysis responds slowly to insulin release and refeeding in starved rats
    • Kee, A. J., Combaret, L., Tilignac, T., Souweine, B., Aurousseau, E., Dalle, M., et al. (2003). Ubiquitin-proteasome-dependent muscle proteolysis responds slowly to insulin release and refeeding in starved rats. J. Physiol 546, 765-776. doi: 10.1113/jphysiol.2002.032367
    • (2003) J. Physiol , vol.546 , pp. 765-776
    • Kee, A.J.1    Combaret, L.2    Tilignac, T.3    Souweine, B.4    Aurousseau, E.5    Dalle, M.6
  • 49
    • 23944494119 scopus 로고    scopus 로고
    • Increased expression of proteasome subunits in skeletal muscle of cancer patients with weight loss
    • Khal, J., Hine, A. V., Fearon, K. C., Dejong, C. H., and Tisdale, M. J. (2005). Increased expression of proteasome subunits in skeletal muscle of cancer patients with weight loss. Int. J. Biochem. Cell Biol . 37, 2196-2206. doi: 10.1016/j.biocel.2004.10.017
    • (2005) Int. J. Biochem. Cell Biol. , vol.37 , pp. 2196-2206
    • Khal, J.1    Hine, A.V.2    Fearon, K.C.3    Dejong, C.H.4    Tisdale, M.J.5
  • 50
    • 34547130325 scopus 로고    scopus 로고
    • Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages
    • Kim, H. T., Kim, K. P., Lledias, F., Kisselev, A. F., Scaglione, K. M., Skowyra, D., et al. (2007). Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages. J. Biol. Chem . 282, 17375-17386. doi: 10.1074/jbc.M609659200
    • (2007) J. Biol. Chem. , vol.282 , pp. 17375-17386
    • Kim, H.T.1    Kim, K.P.2    Lledias, F.3    Kisselev, A.F.4    Scaglione, K.M.5    Skowyra, D.6
  • 51
    • 65249105512 scopus 로고    scopus 로고
    • RAD6-Mediated transcription-coupled H2B ubiquitylation directly stimulates H3K4 methylation in human cells
    • Kim, J., Guermah, M., McGinty, R. K., Lee, J. S., Tang, Z., Milne, T. A., et al. (2009). RAD6-Mediated transcription-coupled H2B ubiquitylation directly stimulates H3K4 methylation in human cells. Cell 137, 459-471. doi: 10.1016/j.cell.2009.02.027
    • (2009) Cell , vol.137 , pp. 459-471
    • Kim, J.1    Guermah, M.2    McGinty, R.K.3    Lee, J.S.4    Tang, Z.5    Milne, T.A.6
  • 52
    • 34250013122 scopus 로고    scopus 로고
    • Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation
    • Knipscheer, P., Van Dijk, W. J., Olsen, J. V., Mann, M., and Sixma, T. K. (2007). Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation. EMBO J . 26, 2797-2807. doi: 10.1038/sj.emboj.7601711
    • (2007) EMBO J. , vol.26 , pp. 2797-2807
    • Knipscheer, P.1    Van Dijk, W.J.2    Olsen, J.V.3    Mann, M.4    Sixma, T.K.5
  • 53
    • 0025998528 scopus 로고
    • Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6
    • Koken, M. H., Reynolds, P., Jaspers-Dekker, I., Prakash, L., Prakash, S., Bootsma, D., et al. (1991). Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6. Proc. Natl. Acad. Sci. U.S.A . 88, 8865-8869. doi: 10.1073/pnas.88.20.8865
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 8865-8869
    • Koken, M.H.1    Reynolds, P.2    Jaspers-Dekker, I.3    Prakash, L.4    Prakash, S.5    Bootsma, D.6
  • 54
    • 84858146420 scopus 로고    scopus 로고
    • Non-canonical ubiquitin-based signals for proteasomal degradation
    • Kravtsova-Ivantsiv, Y., and Ciechanover, A. (2012). Non-canonical ubiquitin-based signals for proteasomal degradation. J. Cell Sci . 125, 539-548. doi: 10.1242/jcs.093567
    • (2012) J. Cell Sci. , vol.125 , pp. 539-548
    • Kravtsova-Ivantsiv, Y.1    Ciechanover, A.2
  • 55
    • 27644438336 scopus 로고    scopus 로고
    • Trim32 is a ubiquitin ligase mutated in limb girdle muscular dystrophy type 2H that binds to skeletal muscle myosin and ubiquitinates actin
    • Kudryashova, E., Kudryashov, D., Kramerova, I., and Spencer, M. J. (2005). Trim32 is a ubiquitin ligase mutated in limb girdle muscular dystrophy type 2H that binds to skeletal muscle myosin and ubiquitinates actin. J. Mol. Biol . 354, 413-424. doi: 10.1016/j.jmb.2005.09.068
    • (2005) J. Mol. Biol. , vol.354 , pp. 413-424
    • Kudryashova, E.1    Kudryashov, D.2    Kramerova, I.3    Spencer, M.J.4
  • 56
    • 84863616612 scopus 로고    scopus 로고
    • TWEAK and TRAF6 regulate skeletal muscle atrophy
    • Kumar, A., Bhatnagar, S., and Paul, P. K. (2012). TWEAK and TRAF6 regulate skeletal muscle atrophy. Curr. Opin. Clin. Nutr. Metab. Care 15, 233-239. doi: 10.1097/MCO.0b013e328351c3fc
    • (2012) Curr. Opin. Clin. Nutr. Metab. Care , vol.15 , pp. 233-239
    • Kumar, A.1    Bhatnagar, S.2    Paul, P.K.3
  • 57
    • 78650652065 scopus 로고    scopus 로고
    • Ser(120) of Ubc2/Rad6 regulates ubiquitin-dependent N-end rule targeting by E3α/Ubr1
    • Kumar, B., Lecompte, K. G., Klein, J. M., and Haas, A. L. (2010). Ser(120) of Ubc2/Rad6 regulates ubiquitin-dependent N-end rule targeting by E3α/Ubr1. J. Biol. Chem . 285, 41300-41309. doi: 10.1074/jbc.M110.169136
    • (2010) J. Biol. Chem. , vol.285 , pp. 41300-41309
    • Kumar, B.1    Lecompte, K.G.2    Klein, J.M.3    Haas, A.L.4
  • 58
    • 0347285363 scopus 로고    scopus 로고
    • Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression
    • Lecker, S. H., Jagoe, R. T., Gilbert, A., Gomes, M., Baracos, V., Bailey, J., et al. (2004). Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression. FASEB J . 18, 39-51. doi: 10.1096/fj.03-0610com
    • (2004) FASEB J. , vol.18 , pp. 39-51
    • Lecker, S.H.1    Jagoe, R.T.2    Gilbert, A.3    Gomes, M.4    Baracos, V.5    Bailey, J.6
  • 59
    • 0032751546 scopus 로고    scopus 로고
    • Ubiquitin conjugation by the N-end rule pathway and mRNAs for its components increase in muscles of diabetic rats
    • Lecker, S. H., Solomon, V., Price, S. R., Kwon, Y. T., Mitch, W. E., and Goldberg, A. L. (1999). Ubiquitin conjugation by the N-end rule pathway and mRNAs for its components increase in muscles of diabetic rats. J. Clin. Invest . 104, 1411-1420. doi: 10.1172/JCI7300
    • (1999) J. Clin. Invest. , vol.104 , pp. 1411-1420
    • Lecker, S.H.1    Solomon, V.2    Price, S.R.3    Kwon, Y.T.4    Mitch, W.E.5    Goldberg, A.L.6
  • 60
    • 0141791457 scopus 로고    scopus 로고
    • Hydrogen peroxide stimulates ubiquitin-conjugating activity and expression of genes for specific E2 and E3 proteins in skeletal muscle myotubes
    • Li, Y. P., Chen, Y., Li, A. S., and Reid, M. B. (2003). Hydrogen peroxide stimulates ubiquitin-conjugating activity and expression of genes for specific E2 and E3 proteins in skeletal muscle myotubes. Am. J. Physiol. Cell Physiol . 285, C806-C812. doi: 10.1152/ajpcell.00129.2003
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285 , pp. C806-C812
    • Li, Y.P.1    Chen, Y.2    Li, A.S.3    Reid, M.B.4
  • 61
    • 13844253851 scopus 로고    scopus 로고
    • Activation of ubiquitin-proteasome pathway is involved in skeletal muscle wasting in a rat model with biliary cirrhosis: potential role of TNF-alpha
    • Lin, S. Y., Chen, W. Y., Lee, F. Y., Huang, C. J., and Sheu, W. H. (2005). Activation of ubiquitin-proteasome pathway is involved in skeletal muscle wasting in a rat model with biliary cirrhosis: potential role of TNF-alpha. Am. J. Physiol. Endocrinol. Metab . 288, E493-E501. doi: 10.1152/ajpendo.00186.2004
    • (2005) Am. J. Physiol. Endocrinol. Metab. , vol.288 , pp. E493-E501
    • Lin, S.Y.1    Chen, W.Y.2    Lee, F.Y.3    Huang, C.J.4    Sheu, W.H.5
  • 62
    • 0031656804 scopus 로고    scopus 로고
    • Mechanism of muscle protein degradation induced by a cancer cachectic factor
    • Lorite, M. J., Thompson, M. G., Drake, J. L., Carling, G., and Tisdale, M. J. (1998). Mechanism of muscle protein degradation induced by a cancer cachectic factor. Br. J. Cancer 78, 850-856. doi: 10.1038/bjc.1998.592
    • (1998) Br. J. Cancer , vol.78 , pp. 850-856
    • Lorite, M.J.1    Thompson, M.G.2    Drake, J.L.3    Carling, G.4    Tisdale, M.J.5
  • 63
    • 25144437375 scopus 로고    scopus 로고
    • A proinflammatory tumor that activates protein degradation sensitizes rats to catabolic effects of endotoxin
    • Mackenzie, M. L., Bedard, N., Wing, S. S., and Baracos, V. E. (2005). A proinflammatory tumor that activates protein degradation sensitizes rats to catabolic effects of endotoxin. Am. J. Physiol. Endocrinol. Metab . 289, E527-E533. doi: 10.1152/ajpendo.00050.2005
    • (2005) Am. J. Physiol. Endocrinol. Metab. , vol.289 , pp. E527-E533
    • Mackenzie, M.L.1    Bedard, N.2    Wing, S.S.3    Baracos, V.E.4
  • 64
    • 0029924205 scopus 로고    scopus 로고
    • Increased mRNA levels for components of the lysosomal, Ca2+-activated, and ATP-ubiquitin-dependent proteolytic pathways in skeletal muscle from head trauma patients
    • Mansoor, O., Beaufrere, B., Boirie, Y., Ralliere, C., Taillandier, D., Aurousseau, E., et al. (1996). Increased mRNA levels for components of the lysosomal, Ca2+-activated, and ATP-ubiquitin-dependent proteolytic pathways in skeletal muscle from head trauma patients. Proc. Natl. Acad. Sci. U.S.A . 93, 2714-2718. doi: 10.1073/pnas.93.7.2714
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 2714-2718
    • Mansoor, O.1    Beaufrere, B.2    Boirie, Y.3    Ralliere, C.4    Taillandier, D.5    Aurousseau, E.6
  • 66
    • 70349645557 scopus 로고    scopus 로고
    • Analysis of the human E2 ubiquitin conjugating enzyme protein interaction network
    • Markson, G., Kiel, C., Hyde, R., Brown, S., Charalabous, P., Bremm, A., et al. (2009). Analysis of the human E2 ubiquitin conjugating enzyme protein interaction network. Genome Res . 19, 1905-1911. doi: 10.1101/gr.093963.109
    • (2009) Genome Res. , vol.19 , pp. 1905-1911
    • Markson, G.1    Kiel, C.2    Hyde, R.3    Brown, S.4    Charalabous, P.5    Bremm, A.6
  • 68
    • 84858142724 scopus 로고    scopus 로고
    • HECT and RING finger families of E3 ubiquitin ligases at a glance
    • Metzger, M. B., Hristova, V. A., and Weissman, A. M. (2012). HECT and RING finger families of E3 ubiquitin ligases at a glance. J. Cell Sci . 125, 531-537. doi: 10.1242/jcs.091777
    • (2012) J. Cell Sci. , vol.125 , pp. 531-537
    • Metzger, M.B.1    Hristova, V.A.2    Weissman, A.M.3
  • 69
    • 84878170491 scopus 로고    scopus 로고
    • A structurally unique E2-binding domain activates ubiquitination by the ERAD E2, Ubc7p, through multiple mechanisms
    • Metzger, M. B., Liang, Y. H., Das, R., Mariano, J., Li, S., Li, J., et al. (2013). A structurally unique E2-binding domain activates ubiquitination by the ERAD E2, Ubc7p, through multiple mechanisms. Mol. Cell 50, 516-527. doi: 10.1016/j.molcel.2013.04.004
    • (2013) Mol. Cell , vol.50 , pp. 516-527
    • Metzger, M.B.1    Liang, Y.H.2    Das, R.3    Mariano, J.4    Li, S.5    Li, J.6
  • 70
    • 67449091213 scopus 로고    scopus 로고
    • What was the set of ubiquitin and ubiquitin-like conjugating enzymes in the eukaryote common ancestor?
    • Michelle, C., Vourc'h, P., Mignon, L., and Andres, C. R. (2009). What was the set of ubiquitin and ubiquitin-like conjugating enzymes in the eukaryote common ancestor? J. Mol. Evol . 68, 616-628. doi: 10.1007/s00239-009-9225-6
    • (2009) J. Mol. Evol , vol.68 , pp. 616-628
    • Michelle, C.1    Vourc'h, P.2    Mignon, L.3    Andres, C.R.4
  • 71
    • 79951540682 scopus 로고    scopus 로고
    • Functional interactions between ubiquitin E2 enzymes and TRIM proteins
    • Napolitano, L. M., Jaffray, E. G., Hay, R. T., and Meroni, G. (2011). Functional interactions between ubiquitin E2 enzymes and TRIM proteins. Biochem. J . 434, 309-319. doi: 10.1042/BJ20101487
    • (2011) Biochem. J. , vol.434 , pp. 309-319
    • Napolitano, L.M.1    Jaffray, E.G.2    Hay, R.T.3    Meroni, G.4
  • 72
    • 66749160236 scopus 로고    scopus 로고
    • Properties of easily releasable myofilaments: are they the first step in myofibrillar protein turnover?
    • Neti, G., Novak, S. M., Thompson, V. F., and Goll, D. E. (2009). Properties of easily releasable myofilaments: are they the first step in myofibrillar protein turnover? Am. J. Physiol. Cell Physiol . 296, C1383-C1390. doi: 10.1152/ajpcell.00022.2009
    • (2009) Am. J. Physiol. Cell Physiol , vol.296 , pp. C1383-C1390
    • Neti, G.1    Novak, S.M.2    Thompson, V.F.3    Goll, D.E.4
  • 73
    • 84903148006 scopus 로고    scopus 로고
    • The ubiquitin-conjugating enzyme, UbcM2, is restricted to monoubiquitylation by a two-fold mechanism that involves backside residues of E2 and Lys48 of ubiquitin
    • Nguyen, L., Plafker, K. S., Starnes, A., Cook, M., Klevit, R. E., and Plafker, S. M. (2014a). The ubiquitin-conjugating enzyme, UbcM2, is restricted to monoubiquitylation by a two-fold mechanism that involves backside residues of E2 and Lys48 of ubiquitin. Biochemistry 53, 4004-4014. doi: 10.1021/bi500072v
    • (2014) Biochemistry , vol.53 , pp. 4004-4014
    • Nguyen, L.1    Plafker, K.S.2    Starnes, A.3    Cook, M.4    Klevit, R.E.5    Plafker, S.M.6
  • 74
    • 84896709030 scopus 로고    scopus 로고
    • Mitsugumin 53 (MG53) ligase ubiquitinates focal adhesion kinase during skeletal myogenesis
    • Nguyen, N., Yi, J. S., Park, H., Lee, J. S., and Ko, Y. G. (2014b). Mitsugumin 53 (MG53) ligase ubiquitinates focal adhesion kinase during skeletal myogenesis. J. Biol. Chem . 289, 3209-3216. doi: 10.1074/jbc.M113.525154
    • (2014) J. Biol. Chem. , vol.289 , pp. 3209-3216
    • Nguyen, N.1    Yi, J.S.2    Park, H.3    Lee, J.S.4    Ko, Y.G.5
  • 75
    • 34848877881 scopus 로고    scopus 로고
    • Functional characterization of Rad18 domains for Rad6, ubiquitin, DNA binding and PCNA modification
    • Notenboom, V., Hibbert, R. G., Van Rossum-Fikkert, S. E., Olsen, J. V., Mann, M., and Sixma, T. K. (2007). Functional characterization of Rad18 domains for Rad6, ubiquitin, DNA binding and PCNA modification. Nucleic Acids Res . 35, 5819-5830. doi: 10.1093/nar/gkm615
    • (2007) Nucleic Acids Res. , vol.35 , pp. 5819-5830
    • Notenboom, V.1    Hibbert, R.G.2    Van Rossum-Fikkert, S.E.3    Olsen, J.V.4    Mann, M.5    Sixma, T.K.6
  • 76
    • 0033548432 scopus 로고    scopus 로고
    • Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction
    • Nuber, U., and Scheffner, M. (1999). Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction. J. Biol. Chem . 274, 7576-7582. doi: 10.1074/jbc.274.11.7576
    • (1999) J. Biol. Chem. , vol.274 , pp. 7576-7582
    • Nuber, U.1    Scheffner, M.2
  • 77
    • 33746379895 scopus 로고    scopus 로고
    • Human homologs of Ubc6p ubiquitin-conjugating enzyme and phosphorylation of HsUbc6e in response to endoplasmic reticulum stress
    • Oh, R. S., Bai, X., and Rommens, J. M. (2006). Human homologs of Ubc6p ubiquitin-conjugating enzyme and phosphorylation of HsUbc6e in response to endoplasmic reticulum stress. J. Biol. Chem . 281, 21480-21490. doi: 10.1074/jbc.M601843200
    • (2006) J. Biol. Chem. , vol.281 , pp. 21480-21490
    • Oh, R.S.1    Bai, X.2    Rommens, J.M.3
  • 78
    • 63049101044 scopus 로고    scopus 로고
    • Regulatory ubiquitylation in response to DNA double-strand breaks
    • Panier, S., and Durocher, D. (2009). Regulatory ubiquitylation in response to DNA double-strand breaks. DNA Repair (Amst.) 8, 436-443. doi: 10.1016/j.dnarep.2009.01.013
    • (2009) DNA Repair (Amst.) , vol.8 , pp. 436-443
    • Panier, S.1    Durocher, D.2
  • 79
    • 84890888103 scopus 로고    scopus 로고
    • Recent progress in elucidating signalling proteolytic pathways in muscle wasting: potential clinical implications
    • Polge, C., Heng, A. E., Combaret, L., Bechet, D., Taillandier, D., and Attaix, D. (2013). Recent progress in elucidating signalling proteolytic pathways in muscle wasting: potential clinical implications. Nutr. Metab. Cardiovasc. Dis . 23(Suppl. 1), S1-S5. doi: 10.1016/j.numecd.2012.08.008
    • (2013) Nutr. Metab. Cardiovasc. Dis. , vol.23 , pp. S1-S5
    • Polge, C.1    Heng, A.E.2    Combaret, L.3    Bechet, D.4    Taillandier, D.5    Attaix, D.6
  • 80
    • 80455174875 scopus 로고    scopus 로고
    • Muscle actin is polyubiquitinylated in vitro and in vivo and targeted for breakdown by the E3 ligase MuRF1
    • Polge, C., Heng, A. E., Jarzaguet, M., Ventadour, S., Claustre, A., Combaret, L., et al. (2011). Muscle actin is polyubiquitinylated in vitro and in vivo and targeted for breakdown by the E3 ligase MuRF1. FASEB J . 25, 3790-3802. doi: 10.1096/fj.11-180968
    • (2011) FASEB J. , vol.25 , pp. 3790-3802
    • Polge, C.1    Heng, A.E.2    Jarzaguet, M.3    Ventadour, S.4    Claustre, A.5    Combaret, L.6
  • 81
    • 84866858702 scopus 로고    scopus 로고
    • Structure of an E3:E2~Ub complex reveals an allosteric mechanism shared among RING/U-box ligases
    • Pruneda, J. N., Littlefield, P. J., Soss, S. E., Nordquist, K. A., Chazin, W. J., Brzovic, P. S., et al. (2012). Structure of an E3:E2~Ub complex reveals an allosteric mechanism shared among RING/U-box ligases. Mol. Cell 47, 933-942. doi: 10.1016/j.molcel.2012.07.001
    • (2012) Mol. Cell , vol.47 , pp. 933-942
    • Pruneda, J.N.1    Littlefield, P.J.2    Soss, S.E.3    Nordquist, K.A.4    Chazin, W.J.5    Brzovic, P.S.6
  • 82
    • 0036087331 scopus 로고    scopus 로고
    • Control of ubiquitination of proteins in rat tissues by ubiquitin conjugating enzymes and isopeptidases
    • Rajapurohitam, V., Bedard, N., and Wing, S. S. (2002). Control of ubiquitination of proteins in rat tissues by ubiquitin conjugating enzymes and isopeptidases. Am. J. Physiol. Endocrinol. Metab . 282, E739-E745. doi: 10.1152/ajpendo.00511.2001
    • (2002) Am. J. Physiol. Endocrinol. Metab. , vol.282 , pp. E739-E745
    • Rajapurohitam, V.1    Bedard, N.2    Wing, S.S.3
  • 83
    • 84860427832 scopus 로고    scopus 로고
    • Ubiquitin and its binding domains
    • Randles, L., and Walters, K. J. (2012). Ubiquitin and its binding domains. Front. Biosci . 17, 2140-2157. doi: 10.2741/4042
    • (2012) Front. Biosci. , vol.17 , pp. 2140-2157
    • Randles, L.1    Walters, K.J.2
  • 84
    • 33947539481 scopus 로고    scopus 로고
    • Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue
    • Ravid, T., and Hochstrasser, M. (2007). Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue. Nat. Cell Biol . 9, 422-427. doi: 10.1038/ncb1558
    • (2007) Nat. Cell Biol. , vol.9 , pp. 422-427
    • Ravid, T.1    Hochstrasser, M.2
  • 85
    • 50149086108 scopus 로고    scopus 로고
    • Diversity of degradation signals in the ubiquitin-proteasome system
    • Ravid, T., and Hochstrasser, M. (2008). Diversity of degradation signals in the ubiquitin-proteasome system. Nat. Rev. Mol. Cell Biol . 9, 679-690. doi: 10.1038/nrm2468
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 679-690
    • Ravid, T.1    Hochstrasser, M.2
  • 86
    • 33344473389 scopus 로고    scopus 로고
    • Atrophy, hypertrophy, and hypoxemia induce transcriptional regulators of the ubiquitin proteasome system in the rat heart
    • Razeghi, P., Baskin, K. K., Sharma, S., Young, M. E., Stepkowski, S., Essop, M. F., et al. (2006). Atrophy, hypertrophy, and hypoxemia induce transcriptional regulators of the ubiquitin proteasome system in the rat heart. Biochem. Biophys. Res. Commun . 342, 361-364. doi: 10.1016/j.bbrc.2006.01.163
    • (2006) Biochem. Biophys. Res. Commun. , vol.342 , pp. 361-364
    • Razeghi, P.1    Baskin, K.K.2    Sharma, S.3    Young, M.E.4    Stepkowski, S.5    Essop, M.F.6
  • 87
    • 34447097834 scopus 로고    scopus 로고
    • Sequential E2s drive polyubiquitin chain assembly on APC targets
    • Rodrigo-Brenni, M. C., and Morgan, D. O. (2007). Sequential E2s drive polyubiquitin chain assembly on APC targets. Cell 130, 127-139. doi: 10.1016/j.cell.2007.05.027
    • (2007) Cell , vol.130 , pp. 127-139
    • Rodrigo-Brenni, M.C.1    Morgan, D.O.2
  • 88
    • 16044372544 scopus 로고    scopus 로고
    • Inactivation of the HR6B ubiquitin-conjugating DNA repair enzyme in mice causes male sterility associated with chromatin modification
    • Roest, H. P., Van Klaveren, J., De Wit, J., Van Gurp, C. G., Koken, M. H., Vermey, M., et al. (1996). Inactivation of the HR6B ubiquitin-conjugating DNA repair enzyme in mice causes male sterility associated with chromatin modification. Cell 86, 799-810. doi: 10.1016/S0092-8674(00)80154-3
    • (1996) Cell , vol.86 , pp. 799-810
    • Roest, H.P.1    Van Klaveren, J.2    De Wit, J.3    Van Gurp, C.G.4    Koken, M.H.5    Vermey, M.6
  • 89
    • 34047212021 scopus 로고    scopus 로고
    • Amino acids and insulin act additively to regulate components of the ubiquitin-proteasome pathway in C2C12 myotubes
    • Sadiq, F., Hazlerigg, D. G., and Lomax, M. A. (2007). Amino acids and insulin act additively to regulate components of the ubiquitin-proteasome pathway in C2C12 myotubes. BMC Mol. Biol . 8:23. doi: 10.1186/1471-2199-8-23
    • (2007) BMC Mol. Biol , vol.8 , pp. 23
    • Sadiq, F.1    Hazlerigg, D.G.2    Lomax, M.A.3
  • 90
    • 34547447215 scopus 로고    scopus 로고
    • Cdc34 C-terminal tail phosphorylation regulates Skp1/cullin/F-box (SCF)-mediated ubiquitination and cell cycle progression
    • Sadowski, M., Mawson, A., Baker, R., and Sarcevic, B. (2007). Cdc34 C-terminal tail phosphorylation regulates Skp1/cullin/F-box (SCF)-mediated ubiquitination and cell cycle progression. Biochem. J . 405, 569-581. doi: 10.1042/BJ20061812
    • (2007) Biochem. J. , vol.405 , pp. 569-581
    • Sadowski, M.1    Mawson, A.2    Baker, R.3    Sarcevic, B.4
  • 91
    • 84885174647 scopus 로고    scopus 로고
    • Protein breakdown in muscle wasting: role of autophagy-lysosome and ubiquitin-proteasome
    • Sandri, M. (2013). Protein breakdown in muscle wasting: role of autophagy-lysosome and ubiquitin-proteasome. Int. J. Biochem. Cell Biol . 45, 2121-2129. doi: 10.1016/j.biocel.2013.04.023
    • (2013) Int. J. Biochem. Cell Biol. , vol.45 , pp. 2121-2129
    • Sandri, M.1
  • 92
    • 0037090823 scopus 로고    scopus 로고
    • Regulation of the ubiquitin-conjugating enzyme hHR6A by CDK-mediated phosphorylation
    • Sarcevic, B., Mawson, A., Baker, R. T., and Sutherland, R. L. (2002). Regulation of the ubiquitin-conjugating enzyme hHR6A by CDK-mediated phosphorylation. EMBO J . 21, 2009-2018. doi: 10.1093/emboj/21.8.2009
    • (2002) EMBO J. , vol.21 , pp. 2009-2018
    • Sarcevic, B.1    Mawson, A.2    Baker, R.T.3    Sutherland, R.L.4
  • 93
    • 79956322553 scopus 로고    scopus 로고
    • Global quantification of mammalian gene expression control
    • Schwanhausser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., et al. (2011). Global quantification of mammalian gene expression control. Nature 473, 337-342. doi: 10.1038/nature10098
    • (2011) Nature , vol.473 , pp. 337-342
    • Schwanhausser, B.1    Busse, D.2    Li, N.3    Dittmar, G.4    Schuchhardt, J.5    Wolf, J.6
  • 94
    • 84874750871 scopus 로고    scopus 로고
    • Corrigendum: Global quantification of mammalian gene expression control
    • Schwanhausser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., et al. (2013). Corrigendum: Global quantification of mammalian gene expression control. Nature 495, 126-127. doi: 10.1038/nature11848
    • (2013) Nature , vol.495 , pp. 126-127
    • Schwanhausser, B.1    Busse, D.2    Li, N.3    Dittmar, G.4    Schuchhardt, J.5    Wolf, J.6
  • 95
    • 40949135212 scopus 로고    scopus 로고
    • Rad6B is a positive regulator of beta-catenin stabilization
    • Shekhar, M. P., Gerard, B., Pauley, R. J., Williams, B. O., and Tait, L. (2008). Rad6B is a positive regulator of beta-catenin stabilization. Cancer Res . 68, 1741-1750. doi: 10.1158/0008-5472.CAN-07-2111
    • (2008) Cancer Res. , vol.68 , pp. 1741-1750
    • Shekhar, M.P.1    Gerard, B.2    Pauley, R.J.3    Williams, B.O.4    Tait, L.5
  • 96
    • 0038526241 scopus 로고    scopus 로고
    • Protein interactions within the N-end rule ubiquitin ligation pathway
    • Siepmann, T. J., Bohnsack, R. N., Tokgoz, Z., Baboshina, O. V., and Haas, A. L. (2003). Protein interactions within the N-end rule ubiquitin ligation pathway. J. Biol. Chem . 278, 9448-9457. doi: 10.1074/jbc.M211240200
    • (2003) J. Biol. Chem. , vol.278 , pp. 9448-9457
    • Siepmann, T.J.1    Bohnsack, R.N.2    Tokgoz, Z.3    Baboshina, O.V.4    Haas, A.L.5
  • 97
    • 11244259394 scopus 로고    scopus 로고
    • Attenuation of proteasome-induced proteolysis in skeletal muscle by Β-hydroxy-Β-methylbutyrate in cancer-induced muscle loss
    • Smith, H. J., Mukerji, P., and Tisdale, M. J. (2005). Attenuation of proteasome-induced proteolysis in skeletal muscle by Β-hydroxy-Β-methylbutyrate in cancer-induced muscle loss. Cancer Res . 65, 277-283.
    • (2005) Cancer Res. , vol.65 , pp. 277-283
    • Smith, H.J.1    Mukerji, P.2    Tisdale, M.J.3
  • 98
    • 0032514735 scopus 로고    scopus 로고
    • Rates of ubiquitin conjugation increase when muscles atrophy, largely through activation of the N-end rule pathway
    • Solomon, V., Baracos, V., Sarraf, P., and Goldberg, A. L. (1998a). Rates of ubiquitin conjugation increase when muscles atrophy, largely through activation of the N-end rule pathway. Proc. Natl. Acad. Sci. U.S.A . 95, 12602-12607. doi: 10.1073/pnas.95.21.12602
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 12602-12607
    • Solomon, V.1    Baracos, V.2    Sarraf, P.3    Goldberg, A.L.4
  • 99
    • 0032566716 scopus 로고    scopus 로고
    • The N-end rule pathway catalyzes a major fraction of the protein degradation in skeletal muscle
    • Solomon, V., Lecker, S. H., and Goldberg, A. L. (1998b). The N-end rule pathway catalyzes a major fraction of the protein degradation in skeletal muscle. J. Biol. Chem . 273, 25216-25222. doi: 10.1074/jbc.273.39.25216
    • (1998) J. Biol. Chem. , vol.273 , pp. 25216-25222
    • Solomon, V.1    Lecker, S.H.2    Goldberg, A.L.3
  • 100
    • 84877020980 scopus 로고    scopus 로고
    • Activation of UbcH5c similar to Ub Is the result of a shift in interdomain motions of the conjugate bound to U-Box E3 Ligase E4B
    • Soss, S. E., Klevit, R. E., and Chazin, W. J. (2013). Activation of UbcH5c similar to Ub Is the result of a shift in interdomain motions of the conjugate bound to U-Box E3 Ligase E4B. Biochemistry 52, 2991-2999. doi: 10.1021/bi3015949
    • (2013) Biochemistry , vol.52 , pp. 2991-2999
    • Soss, S.E.1    Klevit, R.E.2    Chazin, W.J.3
  • 101
    • 49349089823 scopus 로고    scopus 로고
    • The unique N terminus of the UbcH10 E2 enzyme controls the threshold for APC activation and enhances checkpoint regulation of the APC
    • Summers, M. K., Pan, B., Mukhyala, K., and Jackson, P. K. (2008). The unique N terminus of the UbcH10 E2 enzyme controls the threshold for APC activation and enhances checkpoint regulation of the APC. Mol. Cell 31, 544-556. doi: 10.1016/j.molcel.2008.07.014
    • (2008) Mol. Cell , vol.31 , pp. 544-556
    • Summers, M.K.1    Pan, B.2    Mukhyala, K.3    Jackson, P.K.4
  • 102
    • 0025900036 scopus 로고
    • Yeast RAD6 encoded ubiquitin conjugating enzyme mediates protein degradation dependent on the N-end-recognizing E3 enzyme
    • Sung, P., Berleth, E., Pickart, C., Prakash, S., and Prakash, L. (1991). Yeast RAD6 encoded ubiquitin conjugating enzyme mediates protein degradation dependent on the N-end-recognizing E3 enzyme. EMBO J . 10, 2187-2193.
    • (1991) EMBO J. , vol.10 , pp. 2187-2193
    • Sung, P.1    Berleth, E.2    Pickart, C.3    Prakash, S.4    Prakash, L.5
  • 104
    • 0029903175 scopus 로고    scopus 로고
    • Coordinate activation of lysosomal, Ca 2+-activated and ATP-ubiquitin-dependent proteinases in the unweighted rat soleus muscle
    • Taillandier, D., Aurousseau, E., Meynial-Denis, D., Bechet, D., Ferrara, M., Cottin, P., et al. (1996). Coordinate activation of lysosomal, Ca 2+-activated and ATP-ubiquitin-dependent proteinases in the unweighted rat soleus muscle. Biochem. J . 316, 65-72.
    • (1996) Biochem. J. , vol.316 , pp. 65-72
    • Taillandier, D.1    Aurousseau, E.2    Meynial-Denis, D.3    Bechet, D.4    Ferrara, M.5    Cottin, P.6
  • 106
    • 84900018251 scopus 로고    scopus 로고
    • A high-coverage shRNA screen identifies TMEM129 as an E3 ligase involved in ER-associated protein degradation
    • Van De Weijer, M. L., Bassik, M. C., Luteijn, R. D., Voorburg, C. M., Lohuis, M. A., Kremmer, E., et al. (2014). A high-coverage shRNA screen identifies TMEM129 as an E3 ligase involved in ER-associated protein degradation. Nat. Commun . 5, 3832. doi: 10.1038/ncomms4832
    • (2014) Nat. Commun. , vol.5 , pp. 3832
    • Van De Weijer, M.L.1    Bassik, M.C.2    Luteijn, R.D.3    Voorburg, C.M.4    Lohuis, M.A.5    Kremmer, E.6
  • 107
    • 69249150517 scopus 로고    scopus 로고
    • A comprehensive framework of E2-RING E3 interactions of the human ubiquitin-proteasome system
    • Van Wijk, S. J., De Vries, S. J., Kemmeren, P., Huang, A., Boelens, R., Bonvin, A. M., et al. (2009). A comprehensive framework of E2-RING E3 interactions of the human ubiquitin-proteasome system. Mol. Syst. Biol . 5, 295. doi: 10.1038/msb.2009.55
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 295
    • Van Wijk, S.J.1    De Vries, S.J.2    Kemmeren, P.3    Huang, A.4    Boelens, R.5    Bonvin, A.M.6
  • 108
    • 77951651753 scopus 로고    scopus 로고
    • The family of ubiquitin-conjugating enzymes (E2s): deciding between life and death of proteins
    • Van Wijk, S. J., and Timmers, H. T. (2010). The family of ubiquitin-conjugating enzymes (E2s): deciding between life and death of proteins. FASEB J . 24, 981-993. doi: 10.1096/fj.09-136259
    • (2010) FASEB J. , vol.24 , pp. 981-993
    • Van Wijk, S.J.1    Timmers, H.T.2
  • 109
    • 0029883726 scopus 로고    scopus 로고
    • Muscle wasting in a rat model of long-lasting sepsis results from the activation of lysosomal, Ca2+-activated, and ubiquitin-proteasome proteolytic pathways
    • Voisin, L., Breuille, D., Combaret, L., Pouyet, C., Taillandier, D., Aurousseau, E., et al. (1996). Muscle wasting in a rat model of long-lasting sepsis results from the activation of lysosomal, Ca2+-activated, and ubiquitin-proteasome proteolytic pathways. J. Clin. Invest . 97, 1610-1617. doi: 10.1172/JCI118586
    • (1996) J. Clin. Invest. , vol.97 , pp. 1610-1617
    • Voisin, L.1    Breuille, D.2    Combaret, L.3    Pouyet, C.4    Taillandier, D.5    Aurousseau, E.6
  • 110
    • 79957949190 scopus 로고    scopus 로고
    • UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids
    • Wenzel, D. M., Lissounov, A., Brzovic, P. S., and Klevit, R. E. (2011a). UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 474, 105-108. doi: 10.1038/nature09966
    • (2011) Nature , vol.474 , pp. 105-108
    • Wenzel, D.M.1    Lissounov, A.2    Brzovic, P.S.3    Klevit, R.E.4
  • 111
    • 79551493745 scopus 로고    scopus 로고
    • E2s: structurally economical and functionally replete
    • Wenzel, D. M., Stoll, K. E., and Klevit, R. E. (2011b). E2s: structurally economical and functionally replete. Biochem. J . 433, 31-42. doi: 10.1042/BJ20100985
    • (2011) Biochem. J. , vol.433 , pp. 31-42
    • Wenzel, D.M.1    Stoll, K.E.2    Klevit, R.E.3
  • 112
    • 77957284071 scopus 로고    scopus 로고
    • Signaling to NF-kappaB: regulation by ubiquitination. Cold Spring Harb
    • Wertz, I. E., and Dixit, V. M. (2010). Signaling to NF-kappaB: regulation by ubiquitination. Cold Spring Harb. Perspect. Biol . 2:a003350. doi: 10.1101/cshperspect.a003350
    • (2010) Perspect. Biol , vol.2 , pp. a003350
    • Wertz, I.E.1    Dixit, V.M.2
  • 113
    • 0028007982 scopus 로고
    • 14-kDa ubiquitin-conjugating enzyme: structure of the rat gene and regulation upon fasting and by insulin
    • Wing, S. S., and Banville, D. (1994). 14-kDa ubiquitin-conjugating enzyme: structure of the rat gene and regulation upon fasting and by insulin. Am. J. Physiol . 267, E39-E48.
    • (1994) Am. J. Physiol. , vol.267 , pp. E39-E48
    • Wing, S.S.1    Banville, D.2
  • 114
    • 0029806222 scopus 로고    scopus 로고
    • Insulin-like growth factor I stimulates degradation of an mRNA transcript encoding the 14 kDa ubiquitin-conjugating enzyme
    • Wing, S. S., and Bedard, N. (1996). Insulin-like growth factor I stimulates degradation of an mRNA transcript encoding the 14 kDa ubiquitin-conjugating enzyme. Biochem. J . 319, 455-461.
    • (1996) Biochem. J. , vol.319 , pp. 455-461
    • Wing, S.S.1    Bedard, N.2
  • 115
    • 0026701772 scopus 로고
    • A rabbit reticulocyte ubiquitin carrier protein that supports ubiquitin-dependent proteolysis (E214k) is homologous to the yeast DNA repair gene RAD6
    • Wing, S. S., Dumas, F., and Banville, D. (1992). A rabbit reticulocyte ubiquitin carrier protein that supports ubiquitin-dependent proteolysis (E214k) is homologous to the yeast DNA repair gene RAD6. J. Biol. Chem . 267, 6495-6501.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6495-6501
    • Wing, S.S.1    Dumas, F.2    Banville, D.3
  • 116
    • 70350461507 scopus 로고    scopus 로고
    • Building ubiquitin chains: E2 enzymes at work
    • Ye, Y., and Rape, M. (2009). Building ubiquitin chains: E2 enzymes at work. Nat. Rev. Mol. Cell Biol . 10, 755-764. doi: 10.1038/nrm2780
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 755-764
    • Ye, Y.1    Rape, M.2
  • 117
    • 84883166199 scopus 로고    scopus 로고
    • MG53-induced IRS-1 ubiquitination negatively regulates skeletal myogenesis and insulin signalling
    • Yi, J. S., Park, J. S., Ham, Y. M., Nguyen, N., Lee, N. R., Hong, J., et al. (2013). MG53-induced IRS-1 ubiquitination negatively regulates skeletal myogenesis and insulin signalling. Nat. Commun . 4, 2354. doi: 10.1038/ncomms3354
    • (2013) Nat. Commun. , vol.4 , pp. 2354
    • Yi, J.S.1    Park, J.S.2    Ham, Y.M.3    Nguyen, N.4    Lee, N.R.5    Hong, J.6
  • 118
    • 21644478996 scopus 로고    scopus 로고
    • Clenbuterol induces muscle-specific attenuation of atrophy through effects on the ubiquitin-proteasome pathway
    • Yimlamai, T., Dodd, S. L., Borst, S. E., and Park, S. (2005). Clenbuterol induces muscle-specific attenuation of atrophy through effects on the ubiquitin-proteasome pathway. J. Appl. Physiol . (1985) 99, 71-80. doi: 10.1152/japplphysiol.00448.2004
    • (2005) J. Appl. Physiol. (1985) , vol.99 , pp. 71-80
    • Yimlamai, T.1    Dodd, S.L.2    Borst, S.E.3    Park, S.4
  • 119
    • 67349242723 scopus 로고    scopus 로고
    • E2 interaction and dimerization in the crystal structure of TRAF6
    • Yin, Q., Lin, S. C., Lamothe, B., Lu, M., Lo, Y. C., Hura, G., et al. (2009). E2 interaction and dimerization in the crystal structure of TRAF6. Nat. Struct. Mol. Biol . 16, 658-666. doi: 10.1038/nsmb.1605
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 658-666
    • Yin, Q.1    Lin, S.C.2    Lamothe, B.3    Lu, M.4    Lo, Y.C.5    Hura, G.6
  • 120
    • 0035804666 scopus 로고    scopus 로고
    • Identification, tissue expression, and chromosomal position of a novel gene encoding human ubiquitin-conjugating enzyme E2-230k
    • Yokota, T., Nagai, H., Harada, H., Mine, N., Terada, Y., Fujiwara, H., et al. (2001). Identification, tissue expression, and chromosomal position of a novel gene encoding human ubiquitin-conjugating enzyme E2-230k. Gene 267, 95-100. doi: 10.1016/S0378-1119(01)00407-3
    • (2001) Gene , vol.267 , pp. 95-100
    • Yokota, T.1    Nagai, H.2    Harada, H.3    Mine, N.4    Terada, Y.5    Fujiwara, H.6
  • 121
    • 77951876957 scopus 로고    scopus 로고
    • IGF-1 prevents ANG II-induced skeletal muscle atrophy via Akt- and Foxo-dependent inhibition of the ubiquitin ligase atrogin-1 expression
    • Yoshida, T., Semprun-Prieto, L., Sukhanov, S., and Delafontaine, P. (2010). IGF-1 prevents ANG II-induced skeletal muscle atrophy via Akt- and Foxo-dependent inhibition of the ubiquitin ligase atrogin-1 expression. Am. J. Physiol. Heart Circ. Physiol . 298, H1565-H1570. doi: 10.1152/ajpheart.00146.2010
    • (2010) Am. J. Physiol. Heart Circ. Physiol. , vol.298 , pp. H1565-H1570
    • Yoshida, T.1    Semprun-Prieto, L.2    Sukhanov, S.3    Delafontaine, P.4
  • 122
    • 84875913282 scopus 로고    scopus 로고
    • Fine-tuning BMP7 signalling in adipogenesis by UBE2O/E2-230K-mediated monoubiquitination of SMAD6
    • Zhang, X., Zhang, J., Bauer, A., Zhang, L., Selinger, D. W., Lu, C. X., et al. (2013). Fine-tuning BMP7 signalling in adipogenesis by UBE2O/E2-230K-mediated monoubiquitination of SMAD6. EMBO J . 32, 996-1007. doi: 10.1038/emboj.2013.38
    • (2013) EMBO J. , vol.32 , pp. 996-1007
    • Zhang, X.1    Zhang, J.2    Bauer, A.3    Zhang, L.4    Selinger, D.W.5    Lu, C.X.6
  • 123
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • Zheng, N., Wang, P., Jeffrey, P. D., and Pavletich, N. P. (2000). Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 102, 533-539. doi: 10.1016/S0092-8674(00)00057-X
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, P.D.3    Pavletich, N.P.4


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