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钙调蛋白作为 FTO 双氧酶的 Ca2+ 依赖性相互作用蛋白。

Calmodulin as Ca-Dependent Interactor of FTO Dioxygenase.

机构信息

Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland.

Center of Translational Medicine, Warsaw University of Life Sciences, Nowoursynowska 100, 02-797 Warsaw, Poland.

出版信息

Int J Mol Sci. 2021 Oct 8;22(19):10869. doi: 10.3390/ijms221910869.

DOI:10.3390/ijms221910869
PMID:34639211
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8509707/
Abstract

FTO is an -methyladenosine demethylase removing methyl groups from nucleic acids. Several studies indicate the creation of FTO complexes with other proteins. Here, we looked for regulatory proteins recognizing parts of the FTO dioxygenase region. In the Calmodulin (CaM) Target Database, we found the FTO C-domain potentially binding CaM, and we proved this finding experimentally. The interaction was Ca-dependent but independent on FTO phosphorylation. We found that FTO-CaM interaction essentially influences calcium-binding loops in CaM, indicating the presence of two peptide populations-exchanging as CaM alone and differently, suggesting that only one part of CaM interacts with FTO, and the other one reminds free. The modeling of FTO-CaM interaction showed its stable structure when the half of the CaM molecule saturated with Ca interacts with the FTO C-domain, whereas the other part is disconnected. The presented data indicate calmodulin as a new FTO interactor and support engagement of the FTO protein in calcium signaling pathways.

摘要

FTO 是一种 -N6- 甲基腺嘌呤去甲基酶，可从核酸中去除甲基基团。多项研究表明 FTO 可与其他蛋白形成复合物。在这里，我们寻找可识别 FTO 双加氧酶区域部分的调控蛋白。在钙调蛋白（CaM）靶标数据库中，我们发现 FTO C 结构域可能与 CaM 结合，并通过实验证明了这一发现。这种相互作用依赖于 Ca2+，但不依赖于 FTO 磷酸化。我们发现 FTO-CaM 相互作用本质上影响 CaM 中的钙结合环，表明存在两种肽群体-作为 CaM 单独交换和不同交换，这表明只有 CaM 的一部分与 FTO 相互作用，而另一部分则保持游离。FTO-CaM 相互作用的建模表明，当一半的 CaM 分子与 Ca 饱和并与 FTO C 结构域相互作用时，其结构是稳定的，而另一半则断开。目前的数据表明钙调蛋白是 FTO 的一个新的相互作用蛋白，并支持 FTO 蛋白参与钙信号通路。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/daa3/8509707/29ccfa3485e7/ijms-22-10869-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/daa3/8509707/41d609ef0f55/ijms-22-10869-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/daa3/8509707/94f4301c8db1/ijms-22-10869-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/daa3/8509707/651ff0edf7dc/ijms-22-10869-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/daa3/8509707/b4eacde08a1c/ijms-22-10869-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/daa3/8509707/879b216b5dd7/ijms-22-10869-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/daa3/8509707/29ccfa3485e7/ijms-22-10869-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/daa3/8509707/41d609ef0f55/ijms-22-10869-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/daa3/8509707/94f4301c8db1/ijms-22-10869-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/daa3/8509707/651ff0edf7dc/ijms-22-10869-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/daa3/8509707/b4eacde08a1c/ijms-22-10869-g004.jpg
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