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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Physical and functional interactions between ZIP kinase and UbcH5.

Norihiko Ohbayashi1, Katsuya Okada, Shiho Kawakami

  • 1Department of Immunology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-Ku Kita 12 Nishi 6, Sapporo 060-0812, Japan.

Biochemical and Biophysical Research Communications
|June 3, 2008
PubMed
Summary

UbcH5c interacts with and ubiquitinates Zipper-interacting protein kinase (ZIPK), regulating its accumulation in promyelocytic leukemia protein nuclear bodies (PML-NBs). This identifies a novel regulatory mechanism for ZIPK in cellular processes.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Zipper-interacting protein kinase (ZIPK) is a serine/threonine kinase involved in cell death and transcription.
  • ZIPK regulation mechanisms are largely unknown.
  • Previous work linked leukemia inhibitory factor to ZIPK phosphorylation and STAT3 activation.

Purpose of the Study:

  • To identify novel regulatory partners of ZIPK.
  • To elucidate the mechanism by which ZIPK is regulated.
  • To investigate the role of UbcH5c in ZIPK function and localization.

Main Methods:

  • Yeast two-hybrid screening to identify ZIPK-binding partners.
  • Ubiquitination assays to assess ZIPK modification.
  • Small-interfering RNA (siRNA) to reduce UbcH5 expression.
  • Coexpression studies to observe effects on promyelocytic leukemia protein nuclear body (PML-NB) formation.

Main Results:

  • UbcH5c was identified as a novel ZIPK-binding partner.
  • UbcH5c was found to induce ubiquitination of ZIPK.
  • Reduced UbcH5 expression decreased ZIPK ubiquitination.
  • Coexpression of UbcH5c and ZIPK affected PML-NB formation.

Conclusions:

  • UbcH5 regulates ZIPK accumulation in PML-NBs.
  • This regulation occurs through direct interaction with ZIPK and stimulation of its ubiquitination.
  • Identifies a novel ubiquitination-dependent regulatory pathway for ZIPK.