PIAS proteins: pleiotropic interactors associated with SUMO

  • Miia M. Rytinki
  • Sanna Kaikkonen
  • Petri Pehkonen
  • Tiina Jääskeläinen
  • Jorma J. Palvimo
Review

Abstract

The interactions and functions of protein inhibitors of activated STAT (PIAS) proteins are not restricted to the signal transducers and activators of transcription (STATs), but PIAS1, -2, -3 and -4 interact with and regulate a variety of distinct proteins, especially transcription factors. Although the majority of PIAS-interacting proteins are prone to modification by small ubiquitin-related modifier (SUMO) proteins and the PIAS proteins have the capacity to promote the modification as RING-type SUMO ligases, they do not function solely as SUMO E3 ligases. Instead, their effects are often independent of their Siz/PIAS (SP)-RING finger, but dependent on their capability to noncovalently interact with SUMOs or DNA through their SUMO-interacting motif and scaffold attachment factor-A/B, acinus and PIAS domain, respectively. Here, we present an overview of the cellular regulation by PIAS proteins and propose that many of their functions are due to their capability to mediate and facilitate SUMO-linked protein assemblies.

Keywords

Protein inhibitor of activated STAT (PIAS) Small ubiquitin-related modifier (SUMO) SUMOylation (covalent SUMO modification) SUMO-interacting motif (SIM) E3 ligase SP-RING domain Transcription Coregulator 

Supplementary material

18_2009_61_MOESM1_ESM.doc (126 kb)
Supplementary Table 1 (DOC 126 kb)

Copyright information

© Birkhäuser Verlag, Basel/Switzerland 2009

Authors and Affiliations

  • Miia M. Rytinki
    • 1
  • Sanna Kaikkonen
    • 1
  • Petri Pehkonen
    • 2
  • Tiina Jääskeläinen
    • 1
  • Jorma J. Palvimo
    • 1
  1. 1.Institute of Biomedicine/Medical BiochemistryUniversity of KuopioKuopioFinland
  2. 2.Department of BiosciencesUniversity of KuopioKuopioFinland

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