메뉴 건너뛰기




Volumn 26, Issue 1, 2014, Pages 106-120

Ubiquitylation of Autophagy Receptor Optineurin by HACE1 Activates Selective Autophagy for Tumor Suppression

(22)  Liu, Zhengzhao a,b   Chen, Peng a,b   Gao, Hong e   Gu, Yu a,g   Yang, Jiao a,b   Peng, Hong a,b   Xu, Xingxing a,b   Wang, Haifeng a,b   Yang, Meiqiang a   Liu, Xiaoying g   Fan, Libin g   Chen, Shiyao e   Zhou, Jian e   Sun, Yihong e   Ruan, Kangchen a   Cheng, Shuqun f   Komatsu, Masaaki h   White, Eileen i   Li, Lin a   Ji, Hongbin a   more..


Author keywords

[No Author keywords available]

Indexed keywords

HACE1 ENZYME; OPTINEURIN; POLYUBIQUITIN; TUMOR SUPPRESSOR PROTEIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 84904256742     PISSN: 15356108     EISSN: 18783686     Source Type: Journal    
DOI: 10.1016/j.ccr.2014.05.015     Document Type: Article
Times cited : (194)

References (49)
  • 1
    • 45849153870 scopus 로고    scopus 로고
    • The HECT family of E3 ubiquitin ligases: multiple players in cancer development
    • Bernassola F., Karin M., Ciechanover A., Melino G. The HECT family of E3 ubiquitin ligases: multiple players in cancer development. Cancer Cell 2008, 14:10-21.
    • (2008) Cancer Cell , vol.14 , pp. 10-21
    • Bernassola, F.1    Karin, M.2    Ciechanover, A.3    Melino, G.4
  • 4
    • 0141844580 scopus 로고    scopus 로고
    • Structure of the ubiquitin-associated domain of p62 (SQSTM1) and implications for mutations that cause Paget's disease of bone
    • Ciani B., Layfield R., Cavey J.R., Sheppard P.W., Searle M.S. Structure of the ubiquitin-associated domain of p62 (SQSTM1) and implications for mutations that cause Paget's disease of bone. J.Biol. Chem. 2003, 278:37409-37412.
    • (2003) J.Biol. Chem. , vol.278 , pp. 37409-37412
    • Ciani, B.1    Layfield, R.2    Cavey, J.R.3    Sheppard, P.W.4    Searle, M.S.5
  • 8
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields S., Song O. A novel genetic system to detect protein-protein interactions. Nature 1989, 340:245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 9
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 2009, 78:477-513.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 10
    • 2142663061 scopus 로고    scopus 로고
    • Ubiquitin as a central cellular regulator
    • 2p following S32
    • Finley D., Ciechanover A., Varshavsky A. Ubiquitin as a central cellular regulator. Cell 2004, 116:S29-S32. 2p following S32.
    • (2004) Cell , vol.116
    • Finley, D.1    Ciechanover, A.2    Varshavsky, A.3
  • 12
    • 79151483638 scopus 로고    scopus 로고
    • An online survival analysis tool to rapidly assess the effect of 22,277 genes on breast cancer prognosis using microarray data of 1,809 patients
    • Györffy B., Lanczky A., Eklund A.C., Denkert C., Budczies J., Li Q., Szallasi Z. An online survival analysis tool to rapidly assess the effect of 22,277 genes on breast cancer prognosis using microarray data of 1,809 patients. Breast Cancer Res. Treat. 2010, 123:725-731.
    • (2010) Breast Cancer Res. Treat. , vol.123 , pp. 725-731
    • Györffy, B.1    Lanczky, A.2    Eklund, A.C.3    Denkert, C.4    Budczies, J.5    Li, Q.6    Szallasi, Z.7
  • 13
    • 84898639632 scopus 로고    scopus 로고
    • Atomistic autophagy: the structures of cellular self-digestion
    • Hurley J.H., Schulman B.A. Atomistic autophagy: the structures of cellular self-digestion. Cell 2014, 157:300-311.
    • (2014) Cell , vol.157 , pp. 300-311
    • Hurley, J.H.1    Schulman, B.A.2
  • 14
    • 78651282673 scopus 로고    scopus 로고
    • P62 Targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding
    • Itakura E., Mizushima N. p62 Targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding. J.Cell Biol. 2011, 192:17-27.
    • (2011) J.Cell Biol. , vol.192 , pp. 17-27
    • Itakura, E.1    Mizushima, N.2
  • 15
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • Johansen T., Lamark T. Selective autophagy mediated by autophagic adapter proteins. Autophagy 2011, 7:279-296.
    • (2011) Autophagy , vol.7 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 17
    • 84892802083 scopus 로고    scopus 로고
    • The N-terminal methionine of cellular proteins as a degradation signal
    • Kim H.K., Kim R.R., Oh J.H., Cho H., Varshavsky A., Hwang C.S. The N-terminal methionine of cellular proteins as a degradation signal. Cell 2014, 156:158-169.
    • (2014) Cell , vol.156 , pp. 158-169
    • Kim, H.K.1    Kim, R.R.2    Oh, J.H.3    Cho, H.4    Varshavsky, A.5    Hwang, C.S.6
  • 18
    • 67650234499 scopus 로고    scopus 로고
    • NBR1 cooperates with p62 in selective autophagy of ubiquitinated targets
    • Kirkin V., Lamark T., Johansen T., Dikic I. NBR1 cooperates with p62 in selective autophagy of ubiquitinated targets. Autophagy 2009, 5:732-733.
    • (2009) Autophagy , vol.5 , pp. 732-733
    • Kirkin, V.1    Lamark, T.2    Johansen, T.3    Dikic, I.4
  • 19
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin V., McEwan D.G., Novak I., Dikic I. A role for ubiquitin in selective autophagy. Mol. Cell 2009, 34:259-269.
    • (2009) Mol. Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 22
    • 77950495123 scopus 로고    scopus 로고
    • Physiological significance of selective degradation of p62 by autophagy
    • Komatsu M., Ichimura Y. Physiological significance of selective degradation of p62 by autophagy. FEBS Lett. 2010, 584:1374-1378.
    • (2010) FEBS Lett. , vol.584 , pp. 1374-1378
    • Komatsu, M.1    Ichimura, Y.2
  • 25
    • 84883187967 scopus 로고    scopus 로고
    • Emerging roles of E3 ubiquitin ligases in autophagy
    • Kuang E., Qi J., Ronai Z. Emerging roles of E3 ubiquitin ligases in autophagy. Trends Biochem. Sci. 2013, 38:453-460.
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 453-460
    • Kuang, E.1    Qi, J.2    Ronai, Z.3
  • 26
    • 62649096662 scopus 로고    scopus 로고
    • Mechanistic insights into active site-associated polyubiquitination by the ubiquitin-conjugating enzyme Ube2g2
    • Li W., Tu D., Li L., Wollert T., Ghirlando R., Brunger A.T., Ye Y. Mechanistic insights into active site-associated polyubiquitination by the ubiquitin-conjugating enzyme Ube2g2. Proc. Natl. Acad. Sci. USA 2009, 106:3722-3727.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 3722-3727
    • Li, W.1    Tu, D.2    Li, L.3    Wollert, T.4    Ghirlando, R.5    Brunger, A.T.6    Ye, Y.7
  • 33
    • 66449114033 scopus 로고    scopus 로고
    • P62 at the crossroads of autophagy, apoptosis, and cancer
    • Moscat J., Diaz-Meco M.T. p62 at the crossroads of autophagy, apoptosis, and cancer. Cell 2009, 137:1001-1004.
    • (2009) Cell , vol.137 , pp. 1001-1004
    • Moscat, J.1    Diaz-Meco, M.T.2
  • 34
    • 84891745088 scopus 로고    scopus 로고
    • Historical landmarks of autophagy research
    • Ohsumi Y. Historical landmarks of autophagy research. Cell Res. 2014, 24:9-23.
    • (2014) Cell Res. , vol.24 , pp. 9-23
    • Ohsumi, Y.1
  • 37
    • 78049495046 scopus 로고    scopus 로고
    • Ubiquitin accumulation in autophagy-deficient mice is dependent on the Nrf2-mediated stress response pathway: a potential role for protein aggregation in autophagic substrate selection
    • Riley B.E., Kaiser S.E., Shaler T.A., Ng A.C., Hara T., Hipp M.S., Lage K., Xavier R.J., Ryu K.Y., Taguchi K., et al. Ubiquitin accumulation in autophagy-deficient mice is dependent on the Nrf2-mediated stress response pathway: a potential role for protein aggregation in autophagic substrate selection. J.Cell Biol. 2010, 191:537-552.
    • (2010) J.Cell Biol. , vol.191 , pp. 537-552
    • Riley, B.E.1    Kaiser, S.E.2    Shaler, T.A.3    Ng, A.C.4    Hara, T.5    Hipp, M.S.6    Lage, K.7    Xavier, R.J.8    Ryu, K.Y.9    Taguchi, K.10
  • 38
    • 67349132223 scopus 로고    scopus 로고
    • Physiological functions of the HECT family of ubiquitin ligases
    • Rotin D., Kumar S. Physiological functions of the HECT family of ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 2009, 10:398-409.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 398-409
    • Rotin, D.1    Kumar, S.2
  • 41
    • 0035800889 scopus 로고    scopus 로고
    • Methods of detection of vascular reactive species: nitric oxide, superoxide, hydrogen peroxide, and peroxynitrite
    • Tarpey M.M., Fridovich I. Methods of detection of vascular reactive species: nitric oxide, superoxide, hydrogen peroxide, and peroxynitrite. Circ. Res. 2001, 89:224-236.
    • (2001) Circ. Res. , vol.89 , pp. 224-236
    • Tarpey, M.M.1    Fridovich, I.2
  • 43
    • 80051978811 scopus 로고    scopus 로고
    • The predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradation
    • Weissman A.M., Shabek N., Ciechanover A. The predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradation. Nat. Rev. Mol. Cell Biol. 2011, 12:605-620.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 605-620
    • Weissman, A.M.1    Shabek, N.2    Ciechanover, A.3
  • 44
    • 84861526009 scopus 로고    scopus 로고
    • Deconvoluting the context-dependent role for autophagy in cancer
    • White E. Deconvoluting the context-dependent role for autophagy in cancer. Nat. Rev. Cancer 2012, 12:401-410.
    • (2012) Nat. Rev. Cancer , vol.12 , pp. 401-410
    • White, E.1
  • 46
    • 80052570533 scopus 로고    scopus 로고
    • Ras, ROS and proteotoxic stress: a delicate balance
    • Xu W., Trepel J., Neckers L. Ras, ROS and proteotoxic stress: a delicate balance. Cancer Cell 2011, 20:281-282.
    • (2011) Cancer Cell , vol.20 , pp. 281-282
    • Xu, W.1    Trepel, J.2    Neckers, L.3
  • 47
    • 84857387139 scopus 로고    scopus 로고
    • Cellular and molecular biology of optineurin
    • Ying H., Yue B.Y. Cellular and molecular biology of optineurin. Int. Rev. Cell. Mol. Biol. 2012, 294:223-258.
    • (2012) Int. Rev. Cell. Mol. Biol. , vol.294 , pp. 223-258
    • Ying, H.1    Yue, B.Y.2
  • 49
    • 58849167699 scopus 로고    scopus 로고
    • The isolation and characterization of murine macrophages
    • Chapter 14, Unit 14.1
    • Zhang X., Goncalves R., Mosser D.M. The isolation and characterization of murine macrophages. Curr. Protoc. Immunol. 2008, Chapter 14. Unit 14.1.
    • (2008) Curr. Protoc. Immunol.
    • Zhang, X.1    Goncalves, R.2    Mosser, D.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.