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| == Function == | | == Function == |
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| '''Merlin''' (Mer) or Moesin-exrin-radixin-like protein is a unique tumor suppressor that inhibits mitogenic signaling at the membrane-cytoskeleton interface<ref>PMID:21167305</ref>. The FERM domain of Mer regulates cell proliferation in response to adhesive signaling<ref>PMID:24726726</ref>. | | '''Merlin''' (Mer) or '''Moesin-exrin-radixin-like protein''' is a unique tumor suppressor that inhibits mitogenic signaling at the membrane-cytoskeleton interface<ref>PMID:21167305</ref>. The FERM domain of Mer regulates cell proliferation in response to adhesive signaling<ref>PMID:24726726</ref>. |
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| == Disease == | | == Disease == |
Revision as of 07:14, 26 December 2017
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Function
Merlin (Mer) or Moesin-exrin-radixin-like protein is a unique tumor suppressor that inhibits mitogenic signaling at the membrane-cytoskeleton interface[1]. The FERM domain of Mer regulates cell proliferation in response to adhesive signaling[2].
Disease
Neurofibromatosis type 2, characterized by tumors of the nervous system, is the result of loss of the NF2 gene which encodes Mer[3].
Structural highlights
The binding of Mer FERM domain to the C-terminal of HIV-1 Vpr-binding protein results in the inhibition of Mer-mediated suppression of tumorigenesis. The interactions between the proteins are formed by the α-helix and a β-sheet of Mer and a mostly β-sheet of HIV-1 Vpr-binding protein[4].
- ↑ Chen H, Mei L, Zhou L, Zhang X, Guo C, Li J, Wang H, Zhu Y, Zheng Y, Huang L. Moesin-ezrin-radixin-like protein (merlin) mediates protein interacting with the carboxyl terminus-1 (PICT-1)-induced growth inhibition of glioblastoma cells in the nucleus. Int J Biochem Cell Biol. 2011 Apr;43(4):545-55. doi:, 10.1016/j.biocel.2010.12.011. Epub 2010 Dec 15. PMID:21167305 doi:https://dx.doi.org/10.1016/j.biocel.2010.12.011
- ↑ Cooper J, Giancotti FG. Molecular insights into NF2/Merlin tumor suppressor function. FEBS Lett. 2014 Aug 19;588(16):2743-52. doi: 10.1016/j.febslet.2014.04.001. Epub , 2014 Apr 12. PMID:24726726 doi:https://dx.doi.org/10.1016/j.febslet.2014.04.001
- ↑ Morrow KA, Shevde LA. Merlin: the wizard requires protein stability to function as a tumor suppressor. Biochim Biophys Acta. 2012 Dec;1826(2):400-6. doi: 10.1016/j.bbcan.2012.06.005., Epub 2012 Jun 30. PMID:22750751 doi:https://dx.doi.org/10.1016/j.bbcan.2012.06.005
- ↑ Mori T, Gotoh S, Shirakawa M, Hakoshima T. Structural basis of DDB1-and-Cullin 4-associated Factor 1 (DCAF1) recognition by merlin/NF2 and its implication in tumorigenesis by CD44-mediated inhibition of merlin suppression of DCAF1 function. Genes Cells. 2014 Jun 9. doi: 10.1111/gtc.12161. PMID:24912773 doi:https://dx.doi.org/10.1111/gtc.12161
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3D Structures of merlin
Updated on 26-December-2017
3u8z, 1h4r – hMer FERM domain – human
4zrj – hMer FERM + C-terminal domain (mutant)
1isn – mMer FERM domain - mouse
3wa0 – mMer FERM domain + HIV-1 Vpr-binding protein residues 1417-1506
4p7i – mMer FERM domain + HIV-1 Vpr-binding protein residues 998-1058
4zrk – mMer FERM domain + Lats1 peptide
4zri – hMer FERM domain + Lats2 peptide
References
