Abstract
Intermediate filaments require small heat shock protein chaperones to maintain their structural integrity and prevent their aggregation; mutations in these proteins lead to myopathy and cataract.
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αB-crystallin is a sensor for assembly intermediates and for the subunit topology of desmin intermediate filaments
Cell Stress and Chaperones Open Access 03 May 2017
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References
Goldfarb, L.G. et al. Missense mutations in desmin associated with familial cardiac and skeletal myopathy. Nature Genet. 19, 402–403 (1998).
Fuchs, E. & Cleveland, D.W. A structural scaffolding of intermediate filaments in health and disease. Science 279, 514–519 (1998).
Iwaki, T., Kume-Iwaki, A., Liem, R.K.H. & Goldman, J.E. aB-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain. Cell 57, 71–78 (1989).
Vicart, P. et al. A missense mutation in the aB-crystallin chaperone gene causes a desmin-related myopathy. Nature Genet. 20, 92–95 (1998).
Muñoz-Mármol, A.M. et al. A dysfunctional desmin mutation in a patient with severe generalized myopathy. Proc. Natl. Acad. Sci. USA, 95, 11312–11317 (1998).
Nicholl, I.D. & Quinlan, R.A. Chaperone activity of a-crystallins modulates intermediate filament assembly. EMBO J. 13, 945–953 (1994).
Carter, J.M., Hutcheson, A.M. & Quinlan, R.A. In vitro studies on the assembly properties of the lens proteins CP49, CP115: Co-assembly with a-crystallin but not with vimentin. Exp. Eye Res. 60, 181–192 (1995).
Litt, M. et al. Autosomal dominant mutation of congenital cataract associated with a missense mutation in the human a-crystallin gene CRYAA. Hum. Mol. Genet. 7, 471–474 (1998).
Kim, K.K., Kim, R. & Kim, S.H. Crystal structure of a small heat-shock protein. Nature 394, 595–599 (1998).
Boelens, W.C., Croes, Y., de Ruwe, M., de Reu, L. & de Jong, W.W. Negative charges in the C-terminal domain stabilize the αB-crystallin complex. J. Biol. Chem. 273, 28055–28090 (1998).
Muchowski, P.J., Valdez, M.M. & Clark, J.I. αB-crystallin selectively targets intermediate filament proteins during thermal stress. Invest. Ophthalmol. Vis. Sci. 40, in the press.
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Quinlan, R., van den IJssel, P. Fatal attraction: When chaperone turns harlot. Nat Med 5, 25–26 (1999). https://doi.org/10.1038/4704
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DOI: https://doi.org/10.1038/4704
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