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Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1

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Kim, Young Ho, Choi, Cheol Yong, Kim, Yongsok·1999·Proceedings of the National Academy of Sciences

Abstract

Posttranslational modifications such as ubiquitination and phosphorylation play an important role in the regulation of cellular protein function. Homeodomain-interacting protein kinase 2 (HIPK2) is a member of the recently identified family of nuclear protein kinases that act as corepressors for homeodomain transcription factors. Here, we show that HIPK2 is regulated by a ubiquitin-like protein, SUMO-1. We demonstrate that HIPK2 localizes to nuclear speckles (dots) by means of a speckle-retention signal. This speckle-retention signal contains a domain that interacts with a mouse ubiquitin-like protein conjugating (E2) enzyme, mUBC9. In cultured cells, HIPK2 is covalently modified by SUMO-1, and the SUMO-1 modification of HIPK2 correlates with its localization to nuclear speckles (dots). Thus, our results provide firm evidence that the nuclear protein kinase HIPK2 can be covalently modified by SUMO-1, which directs its localization to nuclear speckles (dots).

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Metadata

Authors
Kim, Y. H., Choi, C. Y., & Kim, Y.
Venue
Proceedings of the National Academy of Sciences
Published
1999-10-26
Volume
96
Issue
22
Pages
12350-12355
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2072339454
Cited by
161
References
0
FWCI
5.65
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1. https://app.cochat.ai/papers/10.1073/pnas.96.22.12350
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Kim, Y. H., Choi, C. Y., & Kim, Y. (1999). Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.96.22.12350

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