Structure of a cell polarity regulator, a complex between atypical PKC and Par6 PB1 domains

Yoshinori Hirano, Sosuke Yoshinaga, Ryu Takeya, Nobuo N. Suzuki, Masataka Horiuchi, Motoyuki Kohjima, Hideki Sumimoto, Fuyuhiko Inagaki

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

A complex of atypical PKC and Par6 is a common regulator for cell polarity-related processes, which is an essential clue to evolutionary conserved cell polarity regulation. Here, we determined the crystal structure of the complex of PKCι and Par6α PB1 domains to a resolution of 1.5 Å. Both PB1 domains adopt a ubiquitin fold. PKCι PB1 presents an OPR, PC. and AID (OPCA) motif, 28 amino acid residues with acidic and hydrophobic residues, which interacts with the conserved lysine residue of Par6α PB1 in a front and back manner. On the interface, several salt bridges are formed including the conserved acidic residues on the OPCA motif of PKCι PB1 and the conserved lysine residue on the Par6α PB1. Structural comparison of the PKCι and Par6α PB1 complex with the p40phox and p67phox PB1 domain complex, subunits of neutrophil NADPH oxidase, reveals that the specific interaction is achieved by tilting the interface so that the insertion or extension in the sequence is engaged in the specificity determinant. The PB1 domain develops the interaction surface on the ubiquitin fold to increase the versatility of molecular interaction.

Original languageEnglish
Pages (from-to)9653-9661
Number of pages9
JournalJournal of Biological Chemistry
Volume280
Issue number10
DOIs
Publication statusPublished - Mar 11 2005

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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