Controlling Cell Death through Post-translational Modifications of DED Proteins

Kamil Seyrek, Nikita V. Ivanisenko, Max Richter, Laura K. Hillert, Corinna König, Inna N. Lavrik

Research output: Contribution to journalReview articlepeer-review

Abstract

Apoptosis is a form of programmed cell death, deregulation of which occurs in multiple disorders, including neurodegenerative and autoimmune diseases as well as cancer. The formation of a death-inducing signaling complex (DISC) and death effector domain (DED) filaments are critical for initiation of the extrinsic apoptotic pathway. Post-translational modifications (PTMs) of DED-containing DISC components such as FADD, procaspase-8, and c-FLIP comprise an additional level of apoptosis regulation, which is necessary to overcome the threshold for apoptosis induction. In this review we discuss the influence of PTMs of FADD, procaspase-8, and c-FLIP on DED filament assembly and cell death induction, with a focus on the 3D organization of the DED filament.

Original languageEnglish
Pages (from-to)354-369
Number of pages16
JournalTrends in Cell Biology
Volume30
Issue number5
DOIs
Publication statusPublished - May 2020

Keywords

  • apoptosis
  • DED proteins
  • nitrosylation
  • phosphorylation
  • SUMOylation
  • ubiquitylation
  • EXTRINSIC APOPTOSIS
  • ACTIVATION
  • PHOSPHORYLATION
  • MODEL
  • C-FLIP
  • DEGRADATION
  • CASPASE-8
  • FADD
  • UBIQUITIN-MEDIATED REGULATION
  • REVEALS

Fingerprint Dive into the research topics of 'Controlling Cell Death through Post-translational Modifications of DED Proteins'. Together they form a unique fingerprint.

Cite this