Chapter 12 Experimental Approaches to Investigate the Proteasomal Degradation Pathways Involved in Regulation of Apoptosis

Alan Tseng, Hiroyuki Inuzuka, Daming Gao, Amrik Singh, Wenyi Wei

Research output: Chapter in Book/Report/Conference proceedingChapter

3 Citations (Scopus)

Abstract

Ubiquitin-mediated proteolysis plays a major role in a variety of cellular functions, including cell metabolism, cell cycle progression, cellular response to DNA damage, and programmed cell death. In most cases, the crucial regulators involved in the control of these diverse cellular functions are modified by specific E3 ubiquitin ligases through the attachment of multiple ubiquitin molecules, a signal that triggers the subsequent destruction by the 26S proteasome complex. Recent studies revealed that the proteasomal degradation pathway regulates the cellular apoptosis process on multiple levels. Thus, a better understanding of the molecular mechanisms that underlie the ubiquitination and destruction of these specific regulators of apoptosis will provide us with insight on how apoptosis is properly controlled in normal cells and how tumor cells evade the apoptosis pathways. This chapter provides an overview of the common methods used to examine whether a target protein is ubiquitinated, as well as the protocols to examine how a putative E3 ligase controls the destruction of the target protein.

Original languageEnglish
Title of host publicationProgrammed Cell Death, The Biology and Therapeutic Implications of Cell Death, Part B
EditorsRoya Khosravi-Far, Zahra Zakeri, Richard Lockshin, Mauro Piacentini
Pages205-223
Number of pages19
DOIs
Publication statusPublished - 2008 Sep 26
Externally publishedYes

Publication series

NameMethods in Enzymology
Volume446
ISSN (Print)0076-6879

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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