The 3rd of 4 volumes discusses the position of ubiquitin-mediated protein breakdown in mobile law and body structure. Required studying for molecular biologists, telephone biologists and physiologists with an curiosity within the topic.Content:
Chapter 1 Ubiquitin: a brand new participant within the Peroxisome box (pages 1–20): Astrid Kragt, Rob Benne and Ben Distel
Chapter 2 The Ubiquitin Proteasome process and Muscle improvement (pages 21–47): Johnny Kim and Thorsten Hoppe
Chapter three The COP9 Signalosome: Structural and Biochemical Conservation and Its Roles within the rules of Plant improvement (pages 48–75): Vicente Rubio and Xing Wang Deng
Chapter four Ubiquitin and Protein Sorting to the Lysosome (pages 76–102): John McCullough, Michael J. Clague and Sylvie Urbe
Chapter five ISG15?dependent legislation (pages 103–131): Arthur L. Haas
Chapter 6 The function of the Ubiquitin–Proteasome Pathway within the rules of the mobile Hypoxia reaction (pages 132–148): Koh Nakayama and Ze'ev Ronai
Chapter 7 p97 and Ubiquitin: a fancy tale (pages 149–193): Louise C. Briggs, Ingrid Dreveny, Valerie E. Pye, Fabienne Beuron, Ciaran F. McKeown, Xiaodong Zhang and Paul S. Freemont
Chapter eight Cdc48 (p97) and Its Cofactors (pages 194–211): Alexander Buchberger
Chapter nine Deubiquitinating Enzymes, mobilephone Proliferation, and melanoma (pages 212–231): Rohan T. Baker
Read or Download Protein Degradation: Cell Biology of the Ubiquitin-Proteasome System, Volume 3 PDF
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Extra info for Protein Degradation: Cell Biology of the Ubiquitin-Proteasome System, Volume 3
Sample text
SOCS-box-containing proteins have been implicated in acting as a bridge between specific substrate-binding domains and SCF-like complexes, similar to F-box proteins [61]. Moreover, Ozz-E3 also contains two NHRs (neuralized homology repeats) that represent protein–protein interaction domains which were originally identified in the Drosophila RING-E3 ligase neuralized [52, 62–64]. Although Ozz-E3 is expressed in differentiating myoblasts, it seems that it is required for organized myofibril growth or maintenance but not for myogenesis since Ozz-E3À=À knockout mice do not show an obvious phenotype.
Wing, S. , Leverson, J. , and Liu, Y. C. The tyrosine kinase negative regulator c-Cbl as a RINGtype, E2-dependent ubiquitin-protein ligase. Science 1999, 286, 309–12. , and Fujiki, Y. Molecular anatomy of the peroxin Pex12p: ring finger domain is essential for Pex12p function and interacts with the peroxisometargeting signal type 1-receptor Pex5p and a ring peroxin, Pex10p. J. Biol. Chem. 2000, 275, 25700–10. , and Kunau, W. H. Pex12p of Saccharomyces cerevisiae is a component of a multi-protein complex essential for peroxisomal matrix protein import.
Mutational analysis of the N-terminal topogenic signal of watermelon glyoxysomal malate dehydrogenase using the heterologous host Hansenula polymorpha. Proc. Natl. Acad. Sci. USA 1994, 91, 3151–55. Swinkels, B. , Gould, S. , Bodnar, A. , Rachubinski, R. , and Subramani, S. A novel, cleavable peroxisomal targeting signal at the amino-terminus of the rat 3-ketoacyl-CoA thiolase. EMBO J. 1991, 10, 3255–62. , Franse, M. , and Tabak, H. F. PAS10 is a tetratricopeptiderepeat protein that is essential for the import of most matrix proteins into peroxisomes of Saccharomyces cerevisiae.