Tyrosine kinase 2 interacts with the proapoptotic protein Siva-1 and augments its apoptotic functions

Biochem Biophys Res Commun. 2010 Sep 17;400(2):252-7. doi: 10.1016/j.bbrc.2010.08.051. Epub 2010 Aug 19.

Abstract

Siva-1 is a molecule that has the potential to induce both extrinsic (receptor-mediated) and intrinsic (non-receptor-mediated) apoptosis. Siva-1 binds to CD27, a member of the tumor necrosis factor receptor (TNFR) family, Abl-related gene (ARG), and BCL-X(L), and these partner molecules reportedly enhance the apoptotic properties of Siva-1. In this study, we show that Siva-1 also interacts with a member of the Jak family protein kinases, tyrosine kinase 2 (Tyk2). Siva-1 bound to Tyk2 via its N-terminal region, and Tyk2 phosphorylated Siva-1 at tyrosines 53 and 162. In murine pro-B cells, Ba/F3 cells, expression of Tyk2 augmented Siva-1-induced apoptosis. This augmentation of Siva-1-induced apoptosis was retained regardless of the phosphorylation of Siva-1, but was almost completely prevented by the abrogation of the Tyk2-Siva-1 association. These findings indicate that the interaction between Siva-1 and Tyk2 directly augments the apoptotic activity of Siva-1. Our novel observations suggest that Siva-1 forms a functional complex with Tyk2 and participates in the transduction of signals that inhibit B lymphocyte growth.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apoptosis Regulatory Proteins / genetics
  • Apoptosis Regulatory Proteins / metabolism*
  • Apoptosis*
  • B-Lymphocytes / metabolism
  • B-Lymphocytes / physiology*
  • Cell Line
  • Humans
  • Phosphorylation
  • Protein Structure, Tertiary
  • TYK2 Kinase / metabolism*
  • Two-Hybrid System Techniques
  • Tyrosine / genetics
  • Tyrosine / metabolism

Substances

  • Apoptosis Regulatory Proteins
  • SIVA1 protein, human
  • Tyrosine
  • TYK2 Kinase