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. 2019 Apr 15;54(6):1907–1920. doi: 10.3892/ijo.2019.4786

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Copyright: © Liu et al.

This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.

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INKA2 contains the conserved iBox domain with the PLV tripeptide. (A) Sequence alignments of human INKA1 iBox, INKA2 iBox, and PAK4-AID. Residues shaded in black indicate the identity with INKA1 iBox. Underlined residues indicate the identity with PAK4-AID. (B) Structure of INKA2 (top panel), PAK4 (bottom panel), and deletion mutant proteins used for immunoprecipitation. CRIB, Cdc42- and Rac-interactive binding domain; AID, auto-inhibitory domain. (C) Sequence alignments of INKA2 iBox between different species. Identical residues are shaded in black. INKA2, inka box actin regulator 2; PAK4, p21 (RAC1) activated kinase 4.