DAP-kinase participates in TNF-alpha- and Fas-induced apoptosis and its function requires the death domain

J Cell Biol. 1999 Jul 12;146(1):141-8. doi: 10.1083/jcb.146.1.141.

Abstract

Death-associated protein (DAP)-kinase is a calcium/calmodulin regulated serine/threonine kinase that carries ankyrin repeats, a death domain, and is localized to the cytoskeleton. Here, we report that this kinase is involved in tumor necrosis factor (TNF)-alpha and Fas-induced apoptosis. Expression of DAP-kinase antisense RNA protected cells from killing by anti-Fas/APO-1 agonistic antibodies. Deletion of the death domain abrogated the apoptotic functions of the kinase, thus, documenting for the first time the importance of this protein domain. Overexpression of a fragment encompassing the death domain of DAP-kinase acted as a specific dominant negative mutant that protected cells from TNF-alpha, Fas, and FADD/MORT1-induced cell death. DAP-kinase apoptotic function was blocked by bcl-2 as well as by crmA and p35 inhibitors of caspases, but not by the dominant negative mutants of FADD/MORT1 or of caspase 8. Thus, it functions downstream to the receptor complex and upstream to other caspases. The multidomain structure of this serine/threonine kinase, combined with its involvement in cell death induced by several different triggers, place DAP-kinase at one of the central molecular pathways leading to apoptosis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing*
  • Apoptosis Regulatory Proteins
  • Apoptosis* / drug effects
  • Blotting, Western
  • Calcium-Calmodulin-Dependent Protein Kinases / chemistry*
  • Calcium-Calmodulin-Dependent Protein Kinases / genetics
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
  • Carrier Proteins / genetics
  • Carrier Proteins / physiology
  • Caspase Inhibitors
  • Caspases / genetics
  • Caspases / metabolism
  • Cell Line
  • Death-Associated Protein Kinases
  • Fas-Associated Death Domain Protein
  • Genes, Dominant / genetics
  • Humans
  • Inhibitor of Apoptosis Proteins
  • Mutation
  • Peptide Fragments / chemistry
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism
  • Proto-Oncogene Proteins c-bcl-2 / genetics
  • Proto-Oncogene Proteins c-bcl-2 / physiology
  • RNA, Antisense / genetics
  • RNA, Antisense / physiology
  • Receptors, Tumor Necrosis Factor / genetics
  • Receptors, Tumor Necrosis Factor / physiology
  • Serpins / genetics
  • Serpins / physiology
  • Transfection
  • Tumor Cells, Cultured
  • Tumor Necrosis Factor-alpha / pharmacology*
  • Viral Proteins / genetics
  • Viral Proteins / physiology
  • fas Receptor / genetics
  • fas Receptor / physiology*

Substances

  • Adaptor Proteins, Signal Transducing
  • Apoptosis Regulatory Proteins
  • Carrier Proteins
  • Caspase Inhibitors
  • FADD protein, human
  • Fas-Associated Death Domain Protein
  • Inhibitor of Apoptosis Proteins
  • Peptide Fragments
  • Proto-Oncogene Proteins c-bcl-2
  • RNA, Antisense
  • Receptors, Tumor Necrosis Factor
  • Serpins
  • Tumor Necrosis Factor-alpha
  • Viral Proteins
  • fas Receptor
  • inhibitor of apoptosis, Nucleopolyhedrovirus
  • interleukin-1beta-converting enzyme inhibitor
  • Death-Associated Protein Kinases
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Caspases