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J. Biol. Chem., Vol. 278, Issue 44, 43516-43524, October 31, 2003

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Molecular Recognition in Dimerization between PB1 Domains^*

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

From the Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan, Division of Genome Biology, Cancer Research Institute, Kanazawa University, Kanazawa 920-0934, Japan, and ^¶Department of Structural Biology, Hokkaido University Graduate School of Pharmaceutical Sciences, Sapporo 060-0812, Japan

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 p67^phox and p40^phox 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 p40^phox 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.

Received for publication, June 16, 2003 , and in revised form, August 8, 2003.

^* This work was supported in part by grants-in-aid for scientific research and the National Project on Protein Structural and Functional Analyses from Ministry of Education, Culture, Sports, Science and Technology of Japan, ONO Medical Research Foundation, and the BIRD project, JST Corporation. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^|| To whom correspondence should be addressed. Tel.: 81-92-642-6806; Fax: 81-92-642-6807; E-mail: hsumi{at}bioreg.kyushu-u.ac.jp.

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