The Ubiquitin System in Health and Disease

Stefan Jentsch, Bernhard Haendler (Herausgeber)

Buch | Softcover

XVI, 191 Seiten

2010 | Softcover reprint of hardcover 1st ed. 2009
Springer Berlin (Verlag)
9783642098802 (ISBN)

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The ubiquitin system has two major functions in eukaryotic cells: it r- ulates protein degradation, which is essential for normal cellular fu- tion and for the removal of potentially harmful, damaged, or misfolded proteins, and it controls protein activity by regulating protein protein interactions and subcellullar localization. The ubiquitin system is thus involved in processes as diverse as cell cycle progression, signal tra- duction, gene transcription, and DNA repair. Not surprisingly, defects in the ubiquitin system have been linked with numerous diseases such as cancer, in?ammation, central nervous system disorders, and metabolic dysfunction. Ubiquitin is a highly conserved 76-amino acid protein which is transferred to its target protein in an ATP-dependent manner. This post-translational modi?cation takes place in a hierarchical, three-step fashion involving an E1 ubiquitin-activating enzyme, an E2 ubiquit- conjugating enzyme, and an E3 ubiquitin ligase. Substrate speci?city is predominantly controlled by members of a large family of E3 - zymes, which form complexes with the proteins that will be modi?ed. This ultimately leads to the covalent attachment of the C-terminus of ubiquitin to usually an?-amino group of a lysine residue in the targeted protein. Additional ubiquitin transfer to lysine-48 of ubiquitin itself will form a polyubiquitin chain, which usually targets the conjugate for degradation by the proteasome. By contrast, mono- or polyubiquityla- VI Preface tion involving lysine-63 is normally involved in the control of protein activity. Ubiquitylation can be reverted by deubiquitylating enzymes, of which approximately 95 exist in mammals.

Crosstalk Between the SUMO and Ubiquitin Pathways.- A Tale of Two Giant Proteases.- Molecular Genetics of the Ubiquitin-Proteasome System: Lessons from Yeast.- Less Is More: How Protein Degradation Regulates Muscle Development.- Transcriptional Control and the Ubiquitin-Proteasome System.- Ubiquitination of Myc: Proteasomal Degradation and Beyond.- Regulation of Apoptosis and Cytokinesis by the Anti-apoptotic E2/E3 Ubiquitin-Ligase BRUCE.- Dissecting Roles of Ubiquitination in the p53 Pathway.- Regulation of T Cell Differentiation and Allergic Responses by the E3 Ubiquitin Ligase Itch.- Approaches to Discovering Drugs that Regulate E3 Ubiquitin Ligases.- Inhibiting Hdm2 and Ubiquitin-Activating Enzyme: Targeting the Ubiquitin Conjugating System in Cancer.

Erscheint lt. Verlag	25.11.2010
Reihe/Serie	Ernst Schering Foundation Symposium Proceedings
Zusatzinfo	XVI, 191 p. 39 illus., 32 illus. in color.
Verlagsort	Berlin
Sprache	englisch
Maße	130 x 210 mm
Gewicht	241 g
Themenwelt	Medizin / Pharmazie ► Allgemeines / Lexika
	Medizin / Pharmazie ► Pharmazie
	Medizin / Pharmazie ► Studium ► 1. Studienabschnitt (Vorklinik)
	Naturwissenschaften ► Biologie ► Biochemie
Schlagworte	enzymes • Post-translational modifications • Proteasome • therapy • Ubiquitin
ISBN-13	9783642098802 / 9783642098802
Zustand	Neuware