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

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Introduction (Cabrero et al., 2006). Interestingly, HDAC6 overexpression could be shown to prevent HIV-1 envelope-dependent cell fusion and infection through the deacetylation of α-tubulin (Valenzuela-Fernandez et al., 2005). Furthermore, HDAC6 seems to be involved in osteoclast maturation through interaction with the RhoA- effector mDia2 (Destaing et al., 2005), however, it is interesting to note that HDAC6-deficient mice have only minor differences in bone density (Zhang et al., 2008b). In addition, they display increased levels of α-tubulin and HSP90 acety- lation, although lymphoid development as well as microtubule organization and stability remain remarkably unaffected. Recently, HDAC6 has emerged as a target of the pharmaceutical industry, although whether the observed tumor-selective activity of HDAC6 inhibitors in- deed results from its involvement in the clearance of misfolded proteins – as sug- gested by their synergism with proteasome inhibitors (Hideshima et al., 2005) – remains unclear. Especially as HDAC6 has also been implicated in tumor cell invasion and metastasis through interaction with BRMS1 (breast cancer metastasis suppressor 1, Hurst et al., 2006) and HSP90 deacetylation (Bali et al., 2005; Fiskus et al., 2007), or its involvement in Akt-PP1 (protein phosphatase 1) medi- ated signaling (Brush et al., 2004; Chen et al., 2005; Park et al., 2008). 35
Chapter 1 The UBA domains of NUB1L are required for binding but not for accelerated degradation of the ubiquitin-like modifier FAT10 Gunter Schmidtke, Birte Kalveram, Elvira Weber * , Petra Bochtler ‡ , Sebastian Lukasiak, Mark Steffen Hipp § and Marcus Groettrup Department of Biology, Division of Immunology, University of Constance, 78457 Konstanz, Germany ‡ Present address: IZKF, Department of Internal Medicine I, University of Ulm, 89081 Ulm, Germany * Present address: Department of Biological Sciences, Stanford University, Stanford, CA 94305, USA Journal of Biological Chemistry. 281(29): 20045-20054. July 21, 2006. 36
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: Introduction where the proteasome i
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 (
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90 Chapter 3
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Chapter 3 Figure 23: The model conj
Page 95 and 96:
Chapter 3 HDAC6 is required for the
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Chapter 3 Figure 26: Both ubiquitin
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Chapter 3 also revealed endogenous,
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Chapter 3 and/or its conjugates is
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Chapter 3 (Hipp et al., 2005), pEGF
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Chapter 4 FAT10-deficient mice disp
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Chapter 4 Once the infection is cle
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Chapter 4 As both wild-type as well
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Chapter 4 Peptides. The synthetic p
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Introduction Chapter 5 Antibodies a
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Chapter 5 binant human and mouse GS
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Chapter 5 Figure 34: The antibodies
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Chapter 5 Figure 36: The antibody s
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Discussion 30 years ago, ubiquitin
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Discussion monomeric ubiquitin as w
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Discussion Alternatively, FAT10 cou
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References D. T. Akey, X. Zhu, M. D
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References Y.-H. Chiu, Q. Sun, and
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References S. Gunawardena, L.-S. He
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References J. A. Johnston, M. E. Il
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References F. Lévy, N. Johnsson, T
Page 137 and 138:
References J.-H. Park, H.-S. Jong,
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References P. Schreiner, X. Chen, K
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References S. Vijay-Kumar, C. E. Bu
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Abbreviations aa amino acid AAA ATP
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Amino Acids Alanine Ala A Arginine
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