Caspase-8 function, and phosphorylation, in cell migration

Semin Cell Dev Biol. 2018 Oct;82:105-117. doi: 10.1016/j.semcdb.2018.01.009. Epub 2018 Feb 17.

Abstract

Caspase-8 is involved in a number of cellular functions, with the most well established being the control of cell death. Yet caspase-8 is unique among the caspases in that it acts as an environmental sensor, transducing a range of signals to cells, modulating responses that extend far beyond simple survival. Ranging from the control of apoptosis and necroptosis and gene regulation to cell adhesion and migration, caspase-8 uses proteolytic and non-proteolytic functions to alter cell behavior. Novel interacting partners provide mechanisms for caspase-8 to position itself at signaling nodes that affect a variety of signaling pathways. Here, we examine the catalytic and noncatalytic modes of action by which caspase-8 influences cell adhesion and migration. The mechanisms vary from post-cleavage remodeling of the cytoskeleton to signaling elements that control focal adhesion turnover. This is facilitated by caspase-8 interaction with a host of cell proteins ranging from the proteases caspase-3 and calpain-2 to adaptor proteins such as p85 and Crk, to the Src family of tyrosine kinases.

Keywords: Activity; Adhesion; Apoptosis; Caspase-8; Dimerization; Migration; Necrosis; Tyrosine phosphorylation.

Publication types

  • Review

MeSH terms

  • Animals
  • Caspase 8 / metabolism*
  • Cell Movement
  • Humans
  • Phosphorylation

Substances

  • Caspase 8