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. 2019 Oct 14;13:974. doi: 10.3389/fnins.2019.00974

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Copyright © 2019 Wang, Kaçar Bayram, Sprute, Ozdemir, Cooper, Pergande, Efthymiou, Nedic, Mazaheri, Stumpfe, Azizi Malamiri, Shariati, Zeighami, Bayram, Naghibzadeh, Tajik, Yaşar, Sami Güven, Bibi, Sultan, Salpietro, Houlden, Per, Galehdari, Shalbafan, Jamshidi and Cirak.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Schematic representation of human MTMR2 protein domains (NP 057240.3) and position of the mutations identified so far, generated by Illustrator for Biological Sequences: IBS. In red are the reported novel mutations identified in our study. The MTMR2 long isoform (MTMR2-L), MTMR2 short isoform (MTMR2-S), and MTM1, all contain (Raess et al., 2017) PH-GRAM domain, phosphatase domain, Coiled-Coil domain, and PDZ binding motif. The two MTMR2 protein isoforms differ only in their translation start sites.