Progress in studies on the DEK protein and its involvement in cellular apoptosis

Sci China C Life Sci. 2009 Jul;52(7):637-42. doi: 10.1007/s11427-009-0088-2. Epub 2009 Jul 30.

Abstract

DEK protein is an ubiquitous phosphorylated nuclear protein. Specific binding of DEK to DNA could change the topology of DNA and then affect the gene activity of the underlying DNA sequences. It is speculated that there might be some potential relationship between the stress reaction of cells and DEK proteins. The phosphorylation status of DEK protein is altered during death-receptor-mediated cell apoptosis. Both phosphorylation and poly(ADP-ribosyl)ation could promote the release of DEK from apoptotic nuclei to extracellular environment, and in this case DEK becomes a potential autoantigen of some autoimmune diseases. The available evidence powerfully suggests that DEK protein is closely relevant to apoptosis. The overexpression of DEK protein has dual function in cell apoptosis, in terms of inhibiting or triggering cell apoptosis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Apoptosis / physiology*
  • Autoimmune Diseases / genetics
  • Autoimmune Diseases / physiopathology
  • Caspases / metabolism
  • Chromosomal Proteins, Non-Histone / chemistry
  • Chromosomal Proteins, Non-Histone / genetics
  • Chromosomal Proteins, Non-Histone / physiology*
  • Conserved Sequence
  • DNA Repair
  • Gene Expression Regulation
  • HeLa Cells
  • Humans
  • Nucleoproteins / physiology
  • Oncogene Proteins / chemistry
  • Oncogene Proteins / genetics
  • Oncogene Proteins / physiology*
  • Phosphorylation
  • Poly-ADP-Ribose Binding Proteins
  • Tumor Suppressor Protein p53 / metabolism

Substances

  • Chromosomal Proteins, Non-Histone
  • DEK protein, human
  • Nucleoproteins
  • Oncogene Proteins
  • Poly-ADP-Ribose Binding Proteins
  • Tumor Suppressor Protein p53
  • Caspases