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PIAS proteins: pleiotropic interactors associated with SUMO

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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.

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Acknowledgments

We are grateful to the Academy of Finland, the Finnish Cancer Foundation, Kuopio Graduate School of Molecular Medicine and Sigrid Jusélius Foundation for support.

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Authors and Affiliations

  1. Institute of Biomedicine/Medical Biochemistry, University of Kuopio, Kuopio, Finland

    Miia M. Rytinki, Sanna Kaikkonen, Tiina Jääskeläinen & Jorma J. Palvimo

  2. Department of Biosciences, University of Kuopio, P.O. Box 1627, 70211, Kuopio, Finland

    Petri Pehkonen

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  1. Miia M. Rytinki
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  2. Sanna Kaikkonen
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Correspondence to Jorma J. Palvimo.

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Rytinki, M.M., Kaikkonen, S., Pehkonen, P. et al. PIAS proteins: pleiotropic interactors associated with SUMO. Cell. Mol. Life Sci. 66, 3029–3041 (2009). https://doi.org/10.1007/s00018-009-0061-z

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  • DOI: https://doi.org/10.1007/s00018-009-0061-z

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