Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein

Nature Genetics - Tập 36 Số 4 - Trang 377-381 - 2004
Giles Watts1, Jill Wymer2, Margaret J. Kovach3, Sarju Mehta2, Steven Mumm4, Daniel Darvish5, Alan Pestronk6, Michael P. Whyte4, Virginia Kimonis2
1Division of Genetics, Children's Hospital Boston, 300 Longwood Avenue, Harvard Medical School, Boston, Massachusetts 02115, USA.
2Division of Genetics, Children's Hospital Boston, 300 Longwood Avenue, Harvard Medical School, Boston, USA
3Department of Biological and Environmental Sciences, 215 Holt Hall-Department 2653, University of Tennessee at Chattanooga, Chattanooga, USA
4Division of Bone and Mineral Diseases, Washington University School of Medicine at Barnes-Jewish Hospital, and Center for Metabolic Bone Disease and Molecular Research, Shriners Hospitals for Children, St. Louis, USA
5HIBM Research Group, 16661 Ventura Boulevard, Encino, USA
6Department of Neurology, Washington University School of Medicine, St. Louis, USA

Tóm tắt

Từ khóa


Tài liệu tham khảo

Kimonis, V.E. et al. Clinical and molecular studies in a unique family with autosomal dominant limb-girdle muscular dystrophy and Paget disease of bone. Genet. Med. 2, 232–241 (2000).

Kovach, M.J. et al. Clinical delineation and localization to chromosome 9p13.3-p12 of a unique dominant disorder in four families: hereditary inclusion body myopathy, Paget disease of bone, and frontotemporal dementia. Mol. Genet. Metab. 74, 458–475 (2001).

Eisenberg, I. et al. The UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase gene is mutated in recessive hereditary inclusion body myopathy. Nat. Genet. 29, 83–87 (2001).

Seppala, R., Lehto, V.P. & Gahl, W.A. Mutations in the human UDP-N-acetylglucosamine 2-epimerase gene define the disease sialuria and the allosteric site of the enzyme. Am. J. Hum. Genet. 64, 1563–1569 (1999).

Watts, G.D.J., Thorne, M., Kovach, M.J., Pestronk, A. & Kimonis, V.E. Clinical and Genetic Heterogeneity in Chromosome 9p associated Hereditary Inclusion Body Myopathy: Exclusion of GNE and three other candidate genes. Neuromuscul. Disord. 13, 559–567 (2003).

Beyer, A. Sequence analysis of the AAA protein family. Protein Sci. 6, 2043–2058 (1997).

Dai, R.M. & Li, C.C. Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation. Nat. Cell Biol. 3, 740–744 (2001).

Rape, M. et al. Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Cell 107, 667–677 (2001).

Zhang, X. et al. Structure of the AAA ATPase p97. Mol. Cell 6, 1473–1484 (2000).

Wang, Q., Song, C. & Li, C.C. Hexamerization of p97-VCP is promoted by ATP binding to the D1 domain and required for ATPase and biological activities. Biochem. Biophys. Res. Commun. 300, 253–260 (2003).

Wang, Q., Song, C. & Li, C.C. Molecular perspectives on p97-VCP: progress in understanding its structure and diverse biological function. J. Struct. Biol. advance online published, 19 December 2003 (doi:10.1016/j.jsb.2003.11.014).

Hetzer, M. et al. Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly. Nat. Cell Biol. 3, 1086–1091 (2001).

Rabinovich, E., Kerem, A., Frohlich, K.U., Diamant, N. & Bar-Nun, S. AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol. Cell. Biol. 22, 626–634 (2002).

Rabouille, C. et al. Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro. Cell 92, 603–610 (1998).

Kondo, H. et al. p47 is a cofactor for p97-mediated membrane. Nature 388, 75–78 (1997).

Meyer, H.H., Shorter, J.G., Seemann, J., Pappin, D. & Warren, G. A complex of mammalian ufd1 and npl4 links the ubiquitin and nuclear transport pathways. EMBO J. 19, 2181–2192 (2000).

Jarosch, E., Geiss-Friedlander, R., Meusser, B., Walter, J. & Sommer, T. Protein dislocation from the endoplasmic reticulum—pulling out the suspect. Traffic 3, 530–536 (2002).

Hirabayashi, M. et al. VCP/p97 in abnormal protein aggregates, cytoplasmic vacuoles, and cell death, phenotypes relevant to neurodegeneration. Cell Death Differ. 8, 977–984 (2001).

Kobayashi, T., Tanaka, K., Inoue, K. & Kakizuka, A. Functional ATPase activity of p97/valosin-containing protein (VCP) is required for the quality control of endoplasmic reticulum in neuronally differentiated mammalian PC12 cells. J. Biol. Chem. 277, 47358–47365 (2002).

Higashiyama, H. et al. Identification of ter94, Drosophila VCP, as a modulator of polyglutamine-induced neurodegeneration. Cell Death Differ. 9, 264–273 (2002).

Layfield, R., Alban, A., Mayer, R.J. & Lowe, J. The ubiquitin protein catabolic disorders. Neuropathol. Appl. Neurobiol. 27, 171–179 (2001).

Garcia-Mata, R., Gao, Y.S. & Sztul, E. Hassles with taking out the garbage: aggravating aggresomes. Traffic 3, 388–396 (2002).

Donaldson, K.M. et al. Ubiquitin-mediated sequestration of normal cellular proteins into polyglutamine aggregates P62 and the sequestosome, a novel mechanism for protein metabolism. Proc. Natl. Acad. Sci. USA 100, 8892–8897 (2003).

Wood, J.D., Beaujeux, T.P. & Shaw, P.J. Protein aggregation in motor neurone disorders. Neuropathol. Appl. Neurobiol. 29, 529–545 (2003).

Nagahama, M. et al. SVIP is a novel VCP/p97-interacting protein whose expression causes cell vacuolation. Mol. Biol. Cell 14, 262–273 (2003).

Mizuno, Y., Hori, S., Kakizuka, A. & Okamoto, K. Vacuole-creating protein in neurodegenerative diseases in humans. Neurosci. Lett. 343, 77–80 (2003).

Hocking, L.J. et al. Domain-specific mutations in sequestosome 1 (SQSTM1) cause familial and sporadic Paget's disease. Hum. Mol. Genet. 11, 2735–2739 (2002).

Laurin, N., Brown, J.P., Morissette, J. & Raymond, V. Recurrent mutation of the gene encoding sequestosome 1 (SQSTM1/p62) in Paget disease of bone. Am. J. Hum. Genet. 70, 1582–1588 (2002).

Yabe, H., Singer, F.R., Tucker, W.S. Jr. & Mills, B.G. Paget-like inclusions in osteopetrosis and hereditary neuromuscular and skeletal disease. Eighth Annual Meeting of the American Society of Bone and Mineral Research, A221 (1986).