10.1371/journal.pone.0212518 Dolunay Kelle Dolunay Kelle Koray Kırımtay Koray Kırımtay Ece Selçuk Ece Selçuk Arzu Karabay Arzu Karabay Elk1 affects katanin and spastin proteins via differential transcriptional and post-transcriptional regulations Public Library of Science 2019 post-transcriptional regulations Microtubule spastin protein expressions KATNA 1 methylation results Elk 1 activity microtubule Elk 1 overexpression Elk 1 binding Elk 1 UTR katanin-p 60 Elk 1 SUMOylation KATNA 1 gene encoding katanin-p 60 SPG 4 methylation 2019-02-21 18:46:32 Dataset https://plos.figshare.com/articles/dataset/Elk1_affects_katanin_and_spastin_proteins_via_differential_transcriptional_and_post-transcriptional_regulations/7753940 <div><p>Microtubule severing, which is highly critical for the survival of both mitotic and post-mitotic cells, has to be precisely adjusted by regulating the expression levels of severing proteins, katanin and spastin. Even though severing mechanism is relatively well-studied, there are limited studies for the transcriptional regulation of microtubule severing proteins. In this study, we identified the main regulatory region of <i>KATNA1</i> gene encoding katanin-p60 as 5’ UTR, which has a key role for its expression, and showed Elk1 binding to <i>KATNA1</i>. Furthermore, we identified that Elk1 decreased katanin-p60 and spastin protein expressions, while mRNA levels were increased upon Elk1 overexpression. In addition, SUMOylation is a known post-translational modification regulating Elk1 activity. A previous study suggested that K230, K249, K254 amino acids in the R domain are the main SUMOylation sites; however, we identified that these amino acids are neither essential nor substantial for Elk1 SUMOylation. Also, we determined that <i>KATNA1</i> methylation results in the reduction of Elk1 binding whereas <i>SPG4</i> methylation does not. Together, our findings emphasizing the impacts of both transcriptional and post-transcriptional regulations of katanin-p60 and spastin suggest that Elk1 has a key role for differential expression patterns of microtubule severing proteins, thereby regulating cellular functions through alterations of microtubule organization.</p></div>