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. 2020 Nov 25;10(11):200263. doi: 10.1098/rsob.200263

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© 2020 The Authors.

Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited.

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Figure 1. — Domain architecture and interaction partners of KRIT1. KRIT1 comprises a Nudix domain, three NPx(Y/F) motifs, an ankyrin repeat domain (ARD) and a FERM (band 4.1, ezrin, radixin, moesin) domain. Tubulin binds KRIT1's Nudix domain, ICAP1 binds KRIT1's 1st NPxY motif, SNX17 binds KRIT1's 2nd NPxY motif, CCM2 and CCM2L bind KRIT1's 3rd or potentially 2nd NPxF motif, and HEG1 and Rap1 bind KRIT1's FERM domain. The binding site of α-catenin, β-catenin, AF-6, VE-cadherin and p120 to KRIT1 or whether the interaction is direct or indirect is currently unclear.