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Papers In Press, published online ahead of print August 14, 2003
Medical Institute of Bioregulation, Kyushu University, Fukuoka, Fukuoka 812-8582
Corresponding Author: hsumi{at}bioreg.kyushu-u.ac.jp
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 prote ins Bem1p and Cdc24p. These PB1 domains harbor either a conserved lysine residue at one side or an acidic OPCA motif around the other side: the lysine of p67phox or Bem1p likely binds to the OPCA of p40phox or Cdc24p, respectively, via electrostatic int e ractions. To further know the 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 a PK C 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 used 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. Th us 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.5na
J. Biol. Chem, 10.1074/jbc.M306330200
Submitted on June 16, 2003
Revised on August 8, 2003
Accepted on August 14, 2003
Molecular recognition in dimerization between PB1 domains
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