Moesin

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Revision as of 08:11, 15 October 2020

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spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Disease 3 Relevance 4 Structural highlights Function Moesin (Membrane-Organizing Extension Spike Protein) is a member of the ERM family (Ezrin-Radixin-Moesin) which is important for organizing membrane domains of effector T cells[1]. It plays a role in modification of the actin cytoskeleton[2]. Disease Moesin is involved in the regulation of cell adhesion, polarity and migration by cross-linking between the actin cytoskeleton and plasma membrane and thus regulates hepatic fibrosis[3]. Relevance Reduction of moesin expression in Drosophila brain resulted in prevention of long term memory formation. Structural highlights

3D structures of moesin

3u8z - hMO FERM domain 1-296 - human
1ef1 - hMO FERM domain + C-terminal domain 487-576
1e5w - hMO FERM domain + 1st helix 297-345
6txq - hMO FERM+helical linker domains - Cryo EM
6txs - hMO FERM+helical linker domains + CD44 peptide
1sgh - hMO FERM domain + EBP50 peptide
2i1k, 2i1j - MO - armyworm
4yl8 - MO + Crumbs - Drosophila melanogaster

References

1. ↑ Ansa-Addo EA, Zhang Y, Yang Y, Hussey GS, Howley BV, Salem M, Riesenberg B, Sun S, Rockey DC, Karvar S, Howe PH, Liu B, Li Z. Membrane-organizing protein moesin controls Treg differentiation and antitumor immunity via TGF-beta signaling. J Clin Invest. 2017 Apr 3;127(4):1321-1337. doi: 10.1172/JCI89281. Epub 2017 Mar , 13. PMID:28287407 doi:http://dx.doi.org/10.1172/JCI89281
2. ↑ Freymuth PS, Fitzsimons HL. The ERM protein Moesin is essential for neuronal morphogenesis and long-term memory in Drosophila. Mol Brain. 2017 Aug 29;10(1):41. doi: 10.1186/s13041-017-0322-y. PMID:28851405 doi:http://dx.doi.org/10.1186/s13041-017-0322-y
3. ↑ Karvar S, Ansa-Addo EA, Suda J, Singh S, Zhu L, Li Z, Rockey DC. Moesin, an Ezrin/Radixin/Moesin Family Member, Regulates Hepatic Fibrosis. Hepatology. 2019 Dec 20. doi: 10.1002/hep.31078. PMID:31860744 doi:http://dx.doi.org/10.1002/hep.31078