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Cell Biology of the Ubiquitin-Proteasome System
Mayer, Robert (ed.)
Cell Biology of the Ubiquitin-Proteasome System
ean9783527314355
temáticaBIOQUÍMICA
año Publicación2008
idiomaINGLÉS
editorialWILEY
colecciónPROTEIN DEGRADATION, 3
formatoCARTONÉ


139,00 €


   PEDIR
 
NOVEDAD
 
Últimas novedades
bioquímica
Protein degradation is a major component in cellular metabolism, regulating numerous cell functions, such as the removal of misfolded proteins, growth and cell division, DNA repair, the immune response and the stress response to emergency conditions.
This third volume in the series discusses the role of ubiquitin-mediated protein breakdown in cellular regulation and physiology.
Drawing on the combined knowledge of the world’s leading protein degradation experts, this handy reference includes information on
* deubiquitylating enzymes
* tyrosine kinase receptors
* the COP9/signalosome complex
* regulation of the NFKB system
* ubiquitin in transcription, DNA monitoring and repair, and peroxisomes,
* endocytosis and membrane trafficking
* the ubiquitin-proteasome system in plants and muscle development.
Required reading for molecular biologists, cell biologists and physiologists with an interest in the topic.
indíce
Preface.
List of Contributors.

1 Ubiquitin: A New Player in the Peroxisome Field (Astrid Kragt, Rob Benne, and Ben Distel).

1.1 Introduction.

1.2 Matrix Protein Import into Peroxisomes is Mediated by Cycling Receptors.

1.3 Pex5p is Monoubiquitinated in Wild-type Cells, but Polyubiquitinated in Late-acting pex Mutants.

1.4 Ubiquitination of Pex18p.

1.5 Role for the RING Finger and AAA Peroxins in Pex5p Ubiquitination and Recycling.

1.6 Pex5p Monoubiquitination: A Role in Receptor Recycling.

1.7 Conclusions/Future Prospects.

Acknowledgements.

References.

2 The Ubiquitin Proteasome System and Muscle Development (Johnny Kim and Thorsten Hoppe).

2.1 Introduction.

2.2 Muscle Histology.

2.3 UPS and Developing Muscle.

2.4 UPS and Organizing Muscle.

2.5 UPS and Muscle Destruction or Degeneration.

2.6 Concluding Remarks.

References.

3 The COP9 Signalosome: Structural and Biochemical Conservation and Its Roles in the Regulation of Plant Development (Vicente Rubio and Xing Wang Deng).

3.1 Introduction.

3.2 The Plant COP9 Signalosome.

3.3 CSN Involvement in the Ubiquitinâ Proteasome Pathway.

3.4 Plant CSN Biochemical Activities.

3.5 CSN Functions in Plant Development.

3.6 Conclusions.

References.

4 Ubiquitin and Protein Sorting to the Lysosome (John McCullough, Michael J. Clague, and Sylvie Urbé).

4.1 Introduction.

4.2 Identification of Ubiquitin as an Endosomal Sorting Signal.

4.3 Ubiquitin-mediated Sorting at the Endosome: The MVB Sorting Machinery.

4.4 Ubiquitin Ligases and Endosomal Sorting.

4.5 Endosomal DUBs.

4.6 Polyubiquitin Linkages and Endocytosis.

4.7 Future Directions.

Acknowledgements.

References.

5 ISG15-dependent Regulation (Arthur L. Haas).

5.1 Introduction and Overview.

5.2 The Discovery of ISG15.

5.3 Structure and Properties of the ISG15 Protein.

5.4 The ISG15 Conjugation Pathway.

5.5 Regulation of Intracellular ISG15 Pools.

5.6 Functional Roles for ISG15.

5.7 Perspective.

Acknowledgements.

References.

6 The Role of the Ubiquitinâ Proteasome Pathway in the Regulation of the Cellular Hypoxia Response (Koh Nakayama and Zeâ ™ev Ronai).

6.1 Overview of the Hypoxia Response.

6.2 Players in the Hypoxia-response Signalling Pathway.

6.3 pVHL-dependent Degradation of HIF-1a.

6.4 Siah-dependent Regulation of PHD.

6.5 Other Examples of Altered Ubiquitination During Hypoxia.

6.6 Ischemia Model.

6.7 Regulation of the Ubiquitin System in Hypoxia.

6.8 Concluding Remarks.

References.

7 p97 and Ubiquitin: A Complex Story (Louise C. Briggs, Ingrid Dreveny, Valerie E. Pye, Fabienne Beuron, Ciarán McKeown, Xiaodong Zhang, and Paul S. Freemont).

Abstract.

7.1 Introduction.

7.2 Interactions of Ubiquitin, p97 and Adaptors.

7.3 The Cellular Roles of p97 and Ubiquitin.

7.4 The Action of p97.

7.5 When Things Go Wrong: p97 in Disease.

7.6 Conclusions.

Acknowledgments.

References.

8 Cdc48 (p97) and Its Cofactors (Alexander Buchberger).

8.1 Introduction.

8.2 Cdc48 Cofactors.

8.3 Cellular Functions.

8.4 Outlook.

Acknowledgements.

References.

9 Deubiquitinating Enzymes, Cell Proliferation, and Cancer (Rohan T. Baker).

9.1 Introduction.

9.2 DUBs, Oncogenes, and Cell Transformation.

9.3 Conclusions and Perspectives.

References.

Index.

Finançat per UE