Role of the ubiquitin-like modifier FAT10 in protein degradation and ...

More documents

Recommendations

Info

Discussion the nature of FAT10’s target proteins. In addition, post-mortem brains of pa- tients with Huntington’s or Alzheimer’s disease are being investigated for signs of FAT10 enrichment and FAT10 gene-targeted mice will be utilized to examine the requirement for FAT10 in a drug-induced model of Mallory-Denk body formation. Furthermore, continuing studies investigating the role of FAT10 in lymphocyte homeostasis as well as in the response to a number of additional intracellular pathogens are also being conducted. 125
References D. T. Akey, X. Zhu, M. Dyer, A. Li, A. Sorensen, S. Blackshaw, T. Fukuda-Kamitani, S. P. Daiger, C. M. Craft, T. Kamitani, and M. M. Sohocki. The inherited blindness associated protein AIPL1 interacts with the cell cycle regulator protein NUB1. Hum Mol Genet, 11(22):2723–2733, Oct 2002. S. Alberti, J. Demand, C. Esser, N. Emmerich, H. Schild, and J. Hohfeld. Ubiquitylation of BAG- 1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome. J Biol Chem, 277(48):45920–45927, Nov 2002. B. Alvarez-Castelao and J. G. Castaño. Mechanism of direct degradation of IkappaBalpha by 20S proteasome. FEBS Lett, 579(21):4797–4802, Aug 2005. A. Y. Amerik and M. Hochstrasser. Mechanism and function of deubiquitinating enzymes. Biochim Biophys Acta, 1695(1-3):189–207, Nov 2004. A. N. Antoniou, S. J. Powis, and T. Elliott. Assembly and export of MHC class I peptide ligands. Curr Opin Immunol, 15(1):75–81, Feb 2003. G. Asher, Z. Bercovich, P. Tsvetkov, Y. Shaul, and C. Kahana. 20S proteasomal degradation of ornithine decarboxylase is regulated by NQO1. Mol Cell, 17(5):645–655, Mar 2005. G. Asher, N. Reuven, and Y. Shaul. 20S proteasomes and protein degradation "by default". Bioessays, 28(8):844–849, Aug 2006. J. R. Babu, T. Geetha, and M. W. Wooten. Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation. J Neurochem, 94(1):192–203, Jul 2005. V. P. Badovinac and J. T. Harty. CD8(+) T-cell homeostasis after infection: setting the ’curve’. Microbes Infect, 4(4):441–447, Apr 2002. P. Bali, M. Pranpat, J. Bradner, M. Balasis, W. Fiskus, F. Guo, K. Rocha, S. Kumaraswamy, S. Boyapalle, P. Atadja, E. Seto, and K. Bhalla. Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors. J Biol Chem., 280(29):26729–34. Epub 2005 Jun 2., 2005. M. Basler, N. Youhnovski, M. V. D. Broek, M. Przybylski, and M. Groettrup. Immunoproteasomes down-regulate presentation of a subdominant T cell epitope from lymphocytic choriomeningitis virus. J Immunol, 173(6):3925–3934, Sep 2004. E. E. Bates, O. Ravel, M. C. Dieu, S. Ho, C. Guret, J. M. Bridon, S. Ait-Yahia, F. Brière, C. Caux, J. Banchereau, and S. Lebecque. Identification and analysis of a novel member of the ubiquitin family expressed in dendritic cells and mature B cells. Eur J Immunol, 27(10):2471–2477, Oct 1997. W. Baumeister, J. Walz, F. Zühl, and E. Seemüller. The proteasome: paradigm of a selfcompartmentalizing protease. Cell, 92(3):367–380, Feb 1998. R. Beal, Q. Deveraux, G. Xia, M. Rechsteiner, and C. Pickart. Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting. Proc Natl Acad Sci U S A, 93(2):861– 866, Jan 1996. S. Ben-Shahar, A. Komlosh, E. Nadav, I. Shaked, T. Ziv, A. Admon, G. N. DeMartino, and Y. Reiss. 26 S proteasome-mediated production of an authentic major histocompatibility class I-restricted epitope from an intact protein substrate. J Biol Chem, 274(31):21963–21972, Jul 1999. 126
Page 1 and 2:
Role of the ubiquitin-like modifier
Page 3 and 4:
Acknowledgements . . . . . . . . .
Page 5 and 6:
Summary / Zusammenfassung English F
Page 7 and 8:
Summary In conclusion, these result
Page 9 and 10:
Summary nicht von der katalytischen
Page 11 and 12:
The Ubiquitin-Proteasome-System The
Page 13 and 14:
Introduction Figure 1: The 26S prot
Page 15 and 16:
Introduction are the major source o
Page 17 and 18:
Introduction majority of ubiquitin-
Page 19 and 20:
Introduction example contained in t
Page 21 and 22:
Introduction two modifiers apart fr
Page 23 and 24:
Introduction Figure 4: Comparison o
Page 25 and 26:
Introduction dependent apoptosis in
Page 27 and 28:
Introduction Interestingly, a recen
Page 29 and 30:
The Autophagy-Lysosome System Intro
Page 31 and 32:
Introduction Figure 5: Molecular ma
Page 33 and 34:
Introduction The transport of misfo
Page 35 and 36:
Introduction where the proteasome i
Page 37 and 38:
Chapter 1 The UBA domains of NUB1L
Page 39 and 40:
Introduction Chapter 1 Ubiquitin, a
Page 41 and 42:
Chapter 1 no correlation between th
Page 43 and 44:
Chapter 1 covered proteins were sep
Page 45 and 46:
Chapter 1 Figure 8: Accelerated deg
Page 47 and 48:
Chapter 1 Treatment with IFN-γ and
Page 49 and 50:
Chapter 1 ing SUMO-1-GFP or the C-t
Page 51 and 52:
Chapter 1 Figure 12: Accelerated de
Page 53 and 54:
Chapter 1 Figure 13: Co-immunopreci
Page 55 and 56:
Chapter 1 domains of NUB1L is requi
Page 57 and 58:
Chapter 1 Rad23 (Verma et al., 2004
Page 59 and 60:
Chapter 1 FAT10-GFP expressing vect
Page 61 and 62:
Chapter 2 Degradation of FAT10 by t
Page 63 and 64:
Introduction Chapter 2 The proteaso
Page 65 and 66:
Chapter 2 From our previous data it
Page 67 and 68:
Chapter 2 Figure 14: Purified compo
Page 69 and 70:
Chapter 2 evaluation of the NUB1L b
Page 71 and 72:
Chapter 2 teins which contain intri
Page 73 and 74:
Chapter 2 Combined with our studies
Page 75 and 76: Chapter 2 Recombinant expression of
Page 77 and 78: Chapter 2 et al., 2003), both at a
Page 79 and 80: Abstract Chapter 3 During misfolded
Page 81 and 82: Chapter 3 tion between the UPS and
Page 83 and 84: Chapter 3 Figure 18: HDAC6 interact
Page 85 and 86: Chapter 3 Figure 19: Both the BUZ d
Page 87 and 88: Chapter 3 of HDAC6 was required for
Page 89 and 90: Chapter 3 precipitates with HDAC6 (
Page 91 and 92: 90 Chapter 3
Page 93 and 94: Chapter 3 Figure 23: The model conj
Page 95 and 96: Chapter 3 HDAC6 is required for the
Page 97 and 98: Chapter 3 Figure 26: Both ubiquitin
Page 99 and 100: Chapter 3 also revealed endogenous,
Page 101 and 102: Chapter 3 and/or its conjugates is
Page 103 and 104: Chapter 3 (Hipp et al., 2005), pEGF
Page 105 and 106: Chapter 4 FAT10-deficient mice disp
Page 107 and 108: Chapter 4 Once the infection is cle
Page 109 and 110: Chapter 4 As both wild-type as well
Page 111 and 112: Chapter 4 Peptides. The synthetic p
Page 113 and 114: Introduction Chapter 5 Antibodies a
Page 115 and 116: Chapter 5 binant human and mouse GS
Page 117 and 118: Chapter 5 Figure 34: The antibodies
Page 119 and 120: Chapter 5 Figure 36: The antibody s
Page 121 and 122: Discussion 30 years ago, ubiquitin
Page 123 and 124: Discussion monomeric ubiquitin as w
Page 125: Discussion Alternatively, FAT10 cou
Page 129 and 130: References Y.-H. Chiu, Q. Sun, and
Page 131 and 132: References S. Gunawardena, L.-S. He
Page 133 and 134: References J. A. Johnston, M. E. Il
Page 135 and 136: References F. Lévy, N. Johnsson, T
Page 137 and 138: References J.-H. Park, H.-S. Jong,
Page 139 and 140: References P. Schreiner, X. Chen, K
Page 141 and 142: References S. Vijay-Kumar, C. E. Bu
Page 143 and 144: Abbreviations aa amino acid AAA ATP
Page 145 and 146: Amino Acids Alanine Ala A Arginine
show all

Role of the ubiquitin-like modifier FAT10 in protein degradation and ...

You also want an ePaper? Increase the reach of your titles

Delete template?

Save as template?