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| [[1sgh]] - hMO FERM domain + EBP50 peptide <br /> | | [[1sgh]] - hMO FERM domain + EBP50 peptide <br /> |
| [[2i1k]], [[2i1j]] - MO - armyworm <br /> | | [[2i1k]], [[2i1j]] - MO - armyworm <br /> |
| [[4yl8]] - MO + Crumbs - mouse <br /> | | [[4yl8]] - MO FERM domain + Crumbs - mouse <br /> |
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| == References == | | == References == |
| <references/> | | <references/> |
| [[Category:Topic Page]] | | [[Category:Topic Page]] |
Revision as of 08:36, 15 October 2020
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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
The 3D structure of the complex between FERM domain of the actin-binding moesin and the C-tail domain of cell polarity protein Crumbs shows that the interaction between the 2 proteins involves very few residues[4].
- ↑ 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:https://dx.doi.org/10.1172/JCI89281
- ↑ 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:https://dx.doi.org/10.1186/s13041-017-0322-y
- ↑ 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:https://dx.doi.org/10.1002/hep.31078
- ↑ Wei Z, Li Y, Ye F, Zhang M. Structural basis for the phosphorylation-regulated interaction between the cytoplasmic tail of cell polarity protein Crumbs and the actin binding protein Moesin. J Biol Chem. 2015 Mar 19. pii: jbc.M115.643791. PMID:25792740 doi:https://dx.doi.org/10.1074/jbc.M115.643791
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3D structures of moesin
Updated on 15-October-2020
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 FERM domain + Crumbs - mouse
References
