Structure of human protein kinase C eta (PKCη) C2 domain and identification of phosphorylation sites

Dene R. Littler, John R. Walker, Yi Min She, Patrick J. Finerty, Elena M. Newman, Sirano Dhe-Paganon

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Abstract

Protein kinase C eta (PKCη) is one of several PKC isoforms found in humans. It is a novel PKC isoform in that it is activated by diacylglycerol and anionic phospholipids but not calcium. The crystal structure of the PKCη-C2 domain, which is thought to mediate anionic phospholipid sensing in the protein, was determined at 1.75 Å resolution. The structure is similar to that of the PKC epsilon C2 domain but with significant variations at the putative lipid-binding site. Two serine residues within PKC eta were identified in vitro as potential autophosphorylation sites. In the unphosphorylated structure both serines line the putative lipid-binding site and may therefore play a role in the lipid-regulation of the kinase.

Original languageEnglish
Pages (from-to)1182-1189
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume349
Issue number4
DOIs
Publication statusPublished - 3 Nov 2006
Externally publishedYes

Keywords

  • C2 domain
  • Eta
  • Novel isoform
  • Phosphorylation
  • PKC
  • Protein kinase C
  • Structure
  • X-ray

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