Zeta inhibitory peptide disrupts electrostatic interactions that maintain atypical protein Kinase C in its active conformation on the scaffold p62

Li Chun Lisa Tsai, Lei Xie, Kim Dore, Li Xie, Jason C. Del Rio, Charles C. King, Guillermo Martinez-Ariza, Christopher Hulme, Roberto Malinow, Philip E. Bourne, Alexandra C. Newton

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16 Scopus citations

Abstract

Background: How atypical PKCs are maintained in an active conformation is unknown. Results: We identify an acidic surface on the aPKC scaffold, p62, that tethers the kinase's autoinhibitory pseudosubstrate to allow activity. The biologically active basic peptide, ZIP, competes for binding to this surface, resulting in localized aPKC autoinhibition. Conclusion: P62 tethers aPKCs in an active conformation. Significance: P62 is a molecular target for ZIP.

Original languageEnglish (US)
Pages (from-to)21845-21856
Number of pages12
JournalJournal of Biological Chemistry
Volume290
Issue number36
DOIs
StatePublished - Sep 4 2015

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Tsai, L. C. L., Xie, L., Dore, K., Xie, L., Del Rio, J. C., King, C. C., Martinez-Ariza, G., Hulme, C., Malinow, R., Bourne, P. E., & Newton, A. C. (2015). Zeta inhibitory peptide disrupts electrostatic interactions that maintain atypical protein Kinase C in its active conformation on the scaffold p62. Journal of Biological Chemistry, 290(36), 21845-21856. https://doi.org/10.1074/jbc.M115.676221