Ubiquitination in apoptosis signaling

Ubiquitination in apoptosis signaling

Authors	L.W. van de Kooij
Supervisors	J. Borst
Award date	22-04-2014
ISBN	9789461824264
Number of pages	198
Organisations	Faculty of Science (FNWI) - Swammerdam Institute for Life Sciences (SILS)
Abstract	The work described in this thesis focuses on ubiquitination and protein degradation, with an emphasis on how these processes regulate apoptosis signaling. More specifically, our aims were: 1. To increase the understanding of ubiquitin-mediated regulation of apoptosis signaling. 2. To identify the E3 ubiquitin ligase targeting the apoptosis protein tBidN for unconventional ubiquitination. 3. To delineate the role of N-terminal acetylation in protein degradation.
Document type	PhD thesis
Note	Research conducted at: Universiteit van Amsterdam
Language	English
Downloads	Thesis Cover Title pages Table of contents Chapter 1: General introduction Chapter 2: Polyubiquitination and proteasomal turnover controls the anti-apoptotic activity of Bcl-B Chapter 3: Ubiquitination by the Membrane-associated RING-CH-8 (MARCH-8) ligase controls steady-state cell surface expression of the death receptor tumor necrosis factor-related apoptosis inducing ligand (TRAIL) receptor 1 Chapter 4: The N-end rule ligase UBR2 interacts with the N-terminal fragment of caspase-cleaved Bid and targets it for ubiquitination Chapter 5: N-terminal acetylation stabilizes proteins by blocking N-terminal ubiquitination, and by directly inhibiting proteasomal processing Chapter 6: General discussion Summary Nederlandse samenvatting Curriculum vitae List of publications Dankwoord
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Ubiquitination in apoptosis signaling