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Mol. Cell. Biol., 04 1995, 2304-2310, Vol 15, No. 4
Copyright © 1995, American Society for Microbiology

AH/PH domain-mediated interaction between Akt molecules and its potential role in Akt regulation

K Datta, TF Franke, TO Chan, A Makris, SI Yang, DR Kaplan, DK Morrison, EA Golemis and PN Tsichlis
Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111.

The cytoplasmic serine-threonine protein kinase coded for by the c-akt proto-oncogene features a protein kinase C-like catalytic domain and a unique NH2-terminal domain (AH domain). The AH domain is a member of a domain superfamily whose prototype was observed in pleckstrin (pleckstrin homology, or PH, domain). In this communication, we present evidence that the AH/PH domain is a domain of protein-protein interaction which mediates the formation of Akt protein complexes. The interaction between c-akt AH/PH domains is highly specific, as determined by the failure of this domain to bind AKT2. The AH/PH domain- mediated interactions depend on the integrity of the entire domain. Akt molecules with deletions of the NH2-terminal portion (amino acids 11 to 60) and AH/PH constructs with deletions of the C-terminal portion of this domain (amino acids 107 to 147) fail to interact with c-akt. To determine the significance of these findings, we carried out in vitro kinase assays using Akt immunoprecipitates from serum-starved and serum- starved, platelet-derived growth factor-stimulated NIH 3T3 cells. Addition of maltose-binding protein-AH/PH fusion recombinant protein, which is expected to bind Akt, to the immunoprecipitates from serum- starved cells induced the activation of the Akt kinase.


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