Figure 1

Chemoattractant-mediated transient activation and membrane localization of Akt/PKB is required for efficient chemotaxis to cAMP in Dictyostelium

Ruedi Meili, Charlene Ellsworth, Susan Lee, T.B.K. Reddy, Hui Ma and Richard A Firtel

  • The EMBO Journal (1999) 18, 2092 - 2105
  • doi:10.1093/emboj/18.8.2092
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Sequence, structure and expression of Dictyostelium Akt/PKB. (A) Sequence comparison of Dictyostelium Akt/PKB with human Akt/PKBalpha and Akt/PKBbeta, rat PKBgamma and Drosophila melanogaster PKB (Bellacosa et al., 1991; Coffer and Woodgett, 1991; Jones et al., 1991; Andjelkovic et al., 1995). Putative sites of phosphorylation in the activation loop and the C-terminal end are marked with a #; gray bar, PH domain; black bar, kinase domain. (DDBJ/EMBL/GenBank accession Nos: Dictyostelium Akt/PKB, u15210; D.melanogaster PKB, x83510; human Akt/PKBalpha, m63167; human Akt/PKBbeta, m77198; rat Akt/PKBgamma, d49836) (B) Structure comparison of mammalian, Drosophila and Dictyostelium Akt/PKB. Proteins have an N-terminal PH domain followed by a conserved kinase domain, and a C-terminal regulatory domain. The consensus sequence around the two sites of phosphorylation are shown. (C) Western blot analysis of the developmental pattern of expression of Dictyostelium Akt/PKB. See Materials and methods for details.

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