Molecular Recognition in Dimerization between PB1 Domains

Yukiko Noda, Motoyuki Kohjima, Tomoko Izaki, Kazuhisa Ota, Sosuke Yoshinaga, Fuyuhiko Inagaki, Takashi Ito, Hideki Sumimoto

研究成果: ジャーナルへの寄稿記事

66 引用 (Scopus)

抄録

The PB1 (Phox and Bem 1) domain is a recently identified module that mediates formation of a heterodimeric complex with other PB1 domain, e.g. the complexes between the phagocyte oxidase activators p67phox and p40phox and between the yeast polarity proteins Bem1p and Cdc24p. These PB1 domains harbor either a conserved lysine residue on one side or an acidic OPCA (OPR/PC/AID) motif around the other side; the lysine of p67 phox or Bem1p likely binds to the OPCA of p40phox or Cdc24p, respectively, via electrostatic interactions. To further understand molecular recognition by PB1 domains, here we investigate the interactions mediated by proteins presenting both the lysine and OPCA on a single PB1 domain, namely Par6, atypical protein kinase C (aPKC), and ZIP. Par6 and aPKC form a complex via the interaction of the Par6 lysine with aPKC-OPCA but not via that between the aPKC lysine and Par6-OPCA, thereby localizing to the tight junction of epithelial cells. aPKC also uses its OPCA to interact with ZIP, another protein that has a PB1 domain presenting both the lysine and OPCA, whereas aPKC binds via the conserved lysine to MEK5 in the same manner as ZIP interacts with MEK5. In addition, ZIP can form a homotypic complex via the conserved electrostatic interactions. Thus the PB1 domain appears to be a protein module that fully exploits its two mutually interacting elements in molecular recognition to expand its repertoire of protein-protein interactions.

元の言語英語
ページ(範囲)43516-43524
ページ数9
ジャーナルJournal of Biological Chemistry
278
発行部数44
DOI
出版物ステータス出版済み - 10 31 2003

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Molecular recognition
Dimerization
Lysine
Proteins
Coulomb interactions
Static Electricity
Fungal Proteins
Tight Junctions
Phagocytes
Ports and harbors
4-ethoxymethylene-2-phenyl-2-oxazoline-5-one
Yeast
PKC-3 protein
Oxidoreductases
Epithelial Cells

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Molecular Recognition in Dimerization between PB1 Domains. / Noda, Yukiko; Kohjima, Motoyuki; Izaki, Tomoko; Ota, Kazuhisa; Yoshinaga, Sosuke; Inagaki, Fuyuhiko; Ito, Takashi; Sumimoto, Hideki.

:: Journal of Biological Chemistry, 巻 278, 番号 44, 31.10.2003, p. 43516-43524.

研究成果: ジャーナルへの寄稿記事

Noda, Yukiko ; Kohjima, Motoyuki ; Izaki, Tomoko ; Ota, Kazuhisa ; Yoshinaga, Sosuke ; Inagaki, Fuyuhiko ; Ito, Takashi ; Sumimoto, Hideki. / Molecular Recognition in Dimerization between PB1 Domains. :: Journal of Biological Chemistry. 2003 ; 巻 278, 番号 44. pp. 43516-43524.
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abstract = "The PB1 (Phox and Bem 1) domain is a recently identified module that mediates formation of a heterodimeric complex with other PB1 domain, e.g. the complexes between the phagocyte oxidase activators p67phox and p40phox and between the yeast polarity proteins Bem1p and Cdc24p. These PB1 domains harbor either a conserved lysine residue on one side or an acidic OPCA (OPR/PC/AID) motif around the other side; the lysine of p67 phox or Bem1p likely binds to the OPCA of p40phox or Cdc24p, respectively, via electrostatic interactions. To further understand molecular recognition by PB1 domains, here we investigate the interactions mediated by proteins presenting both the lysine and OPCA on a single PB1 domain, namely Par6, atypical protein kinase C (aPKC), and ZIP. Par6 and aPKC form a complex via the interaction of the Par6 lysine with aPKC-OPCA but not via that between the aPKC lysine and Par6-OPCA, thereby localizing to the tight junction of epithelial cells. aPKC also uses its OPCA to interact with ZIP, another protein that has a PB1 domain presenting both the lysine and OPCA, whereas aPKC binds via the conserved lysine to MEK5 in the same manner as ZIP interacts with MEK5. In addition, ZIP can form a homotypic complex via the conserved electrostatic interactions. Thus the PB1 domain appears to be a protein module that fully exploits its two mutually interacting elements in molecular recognition to expand its repertoire of protein-protein interactions.",
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AU - Izaki, Tomoko

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AU - Ito, Takashi

AU - Sumimoto, Hideki

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