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J. Biol. Chem., Vol. 278, Issue 36, 34568-34581, September 5, 2003
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¶ ¶ ¶ **
From the
Biochemistry Department, Institute of
Medical Biology and ||Department of Pharmacology,
Institute of Pharmacy, University of Tromsø, 9037 Tromsø,
Norway
The Phox and Bem1p (PB1) domain constitutes a recently recognized
protein-protein interaction domain found in the atypical protein kinase C
(aPKC) isoenzymes, 
/
- and 
PKC; members of
mitogen-activated protein kinase (MAPK) modules like MEK5, MEKK2, and MEKK3;
and in several scaffold proteins involved in cellular signaling. Among the
last group, p62 and Par6 (partitioning-defective 6) are
involved in coupling the aPKCs to signaling pathways involved in cell
survival, growth control, and cell polarity. By mutation analyses and
molecular modeling, we have identified critical residues at the interaction
surfaces of the PB1 domains of aPKCs and p62. A basic charge cluster interacts
with an acidic loop and helix both in p62 oligomerization and in the aPKC-p62
interaction. Subsequently, we determined the abilities of mammalian PB1 domain
proteins to form heteromeric and homomeric complexes mediated by this domain.
We report several novel interactions within this family. An interaction
between the cell polarity scaffold protein Par6 and MEK5 was found.
Furthermore, p62 interacts both with MEK5 and NBR1 in addition to the aPKCs.
Evidence for involvement of p62 in MEK5-ERK5 signaling is presented.
Received for publication, March 28, 2003 , and in revised form, May 7, 2003.
* This work was supported by grants from the "Top Research Programme" of the Norwegian Research Council, the Norwegian Cancer Society, the Aakre Foundation, and the Blix Foundation (to T. J.). 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.
Fellow of the Norwegian Research Council.
¶ These authors contributed equally to this work.
** To whom correspondence should be addressed: Dept. of Biochemistry, Institute of Medical Biology, University of Tromsø, 9037 Tromsø, Norway. Tel.: 47-776-44720; Fax: 47-776-45350; E-mail: terjej{at}fagmed.uit.no.
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