1isn

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Crystal structure of merlin FERM domain

Structural highlights

1isn is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MERL_MOUSE Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex (By similarity). Plays a role in lens development and is required for complete fiber cell terminal differentiation, maintenance of cell polarity and separation of the lens vesicle from the corneal epithelium.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Neurofibromatosis type 2 (NF2) is a dominantly inherited disease associated with the central nervous system. The NF2 gene product merlin is a tumor suppressor, and its mutation or inactivation causes this disease. We report here the crystal structure of the merlin FERM domain containing a 22-residue alpha-helical segment. The structure reveals that the merlin FERM domain consists of three subdomains displaying notable features of the electrostatic surface potentials, although the overall surface potentials similar to those of ezrin/radixin/moesin (ERM) proteins indicate electrostatic membrane association. The structure also is consistent with inactivation mechanisms caused by the pathogenic mutations associated with NF2.

Structural basis for neurofibromatosis type 2. Crystal structure of the merlin FERM domain.,Shimizu T, Seto A, Maita N, Hamada K, Tsukita S, Tsukita S, Hakoshima T J Biol Chem. 2002 Mar 22;277(12):10332-6. Epub 2001 Dec 27. PMID:11756419[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
25 reviews cite this structure
ERM proteins and merlin: integrators at the cell cortex.
Bretscher et al. (2002)
24 more
40 other articles
No citations found

See Also

References

  1. ↑ Wiley LA, Dattilo LK, Kang KB, Giovannini M, Beebe DC. The tumor suppressor merlin is required for cell cycle exit, terminal differentiation, and cell polarity in the developing murine lens. Invest Ophthalmol Vis Sci. 2010 Jul;51(7):3611-8. doi: 10.1167/iovs.09-4371. Epub, 2010 Feb 24. PMID:20181838 doi:http://dx.doi.org/10.1167/iovs.09-4371
  2. ↑ Shimizu T, Seto A, Maita N, Hamada K, Tsukita S, Tsukita S, Hakoshima T. Structural basis for neurofibromatosis type 2. Crystal structure of the merlin FERM domain. J Biol Chem. 2002 Mar 22;277(12):10332-6. Epub 2001 Dec 27. PMID:11756419 doi:10.1074/jbc.M109979200

Contents


PDB ID 1isn

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OCA

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