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J. Biol. Chem., Vol. 276, Issue 5, 3188-3194, February 2, 2001
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§¶ and¶
**
From the Huntington's disease is caused by an expanded
CAG trinucleotide repeat coding for a polyglutamine stretch within the
huntingtin protein. Currently, the function of normal huntingtin and
the mechanism by which expanded huntingtin causes selective
neurotoxicity remain unknown. Clues may come from the identification of
huntingtin-associated proteins (HAPs). Here, we show that huntingtin
copurifies with a single novel 40-kDa protein termed HAP40. HAP40 is
encoded by the open reading frame factor VIII-associated gene A (F8A)
located within intron 22 of the factor VIII gene. In transfected
cell extracts, HAP40 coimmunoprecipitates with full-length huntingtin but not with an N-terminal huntingtin fragment. Recombinant HAP40 is
cytoplasmic in the presence of huntingtin but is actively targeted to
the nucleus in the absence of huntingtin. These data indicate that
HAP40 is likely to contribute to the function of normal huntingtin and
is a candidate for involvement in the aberrant nuclear localization of
mutant huntingtin found in degenerating neurons in Huntington's disease.
Laboratory of Molecular Neurobiology,
Division of Neurobiology, Department of Psychiatry,
Department of Neuroscience, and ** The Program in Cellular and
Molecular Medicine, The Johns Hopkins University School of
Medicine, Baltimore, Maryland 21205-2196
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF299331.
§ Supported by a Huntington's Disease Society of America postdoctoral fellowship. ¶ To whom correspondence may be addressed: Laboratory of Molecular Neurobiology, Departments of Psychiatry and Neuroscience, Johns Hopkins University School of Medicine, Ross 618, 720 Rutland Ave., Baltimore, MD 21205-2196. Tel.: 410-614-0011; Fax: 410-614-0013; E-mail: mfpeters@jhmi.edu (M. F. P.) or caross{at}jhu.edu (C. A. R.).This article has been cited by other articles:
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  A. Pal, F. Severin, B. Lommer, A. Shevchenko, and M. Zerial Huntingtin-HAP40 complex is a novel Rab5 effector that regulates early endosome motility and is up-regulated in Huntington's disease. J. Cell Biol., February 13, 2006; 172(4): 605 - 618. [Abstract] [Full Text] [PDF]
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 R. D. Bagnall, K. L. Ayres, P. M. Green, and F. Giannelli Gene conversion and evolution of Xq28 duplicons involved in recurring inversions causing severe hemophilia A Genome Res., February 1, 2005; 15(2): 214 - 223. [Abstract] [Full Text] [PDF]
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 M. A. Poirier, H. Li, J. Macosko, S. Cai, M. Amzel, and C. A. Ross Huntingtin Spheroids and Protofibrils as Precursors in Polyglutamine Fibrilization J. Biol. Chem., October 18, 2002; 277(43): 41032 - 41037. [Abstract] [Full Text] [PDF]
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 J. N. Lozier, A. Dutra, E. Pak, N. Zhou, Z. Zheng, T. C. Nichols, D. A. Bellinger, M. Read, and R. A. Morgan The Chapel Hill hemophilia A dog colony exhibits a factor VIII gene inversion PNAS, October 1, 2002; 99(20): 12991 - 12996. [Abstract] [Full Text] [PDF]
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 S Davies and D B Ramsden Huntington's disease Mol. Pathol., December 1, 2001; 54(6): 409 - 413. [Abstract] [Full Text] [PDF]
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