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Wild-Type and Mutant Huntingtins Function in Vesicle Trafficking in the Secretory and Endocytic Pathways

Velier, James, Kim, Manho, Schwarz, Cordula, Kim, Tae Wan, Sapp, Ellen, Chase, Kathryn, Aronin, Neil, DiFiglia, Marian·1998·Experimental Neurology
DOI 10.1006/exnr.1998.6832
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Abstract

Huntingtin is a cytoplasmic protein that is found in neurons and somatic cells. In patients with Huntington's disease (HD), the NH2-terminal region of huntingtin has an expanded polyglutamine tract. An abnormal protein interaction by mutant huntingtin has been proposed as a mechanism for HD pathogenesis. Huntingtin associates with vesicle membranes and interacts with proteins involved in vesicle trafficking. It is unclear where along vesicle transport pathways wild-type and mutant huntingtins are found and whether polyglutamine expansion affects this localization. To distinguish wild-type and mutant huntingtin, fibroblasts from normals and HD patients with two mutant alleles (homozygotes) were examined. Immunofluorescence confocal microscopy showed that mutant huntingtin localized with clathrin in membranes of the trans Golgi network and in clathrin-coated and noncoated endosomal vesicles in the cytoplasm and along plasma membranes. Separation of organelles in Nycodenz gradients showed that in normal and HD homozygote patient cells, huntingtin was present in membrane fractions enriched in clathrin. Similar results were obtained in fibroblasts from heterozyote juvenile HD patients who had a highly expanded polyglutamine tract in the HD allele. Western blot analysis of membrane fractions from rat brain showed that wild-type huntingtin was present in fractions that contained purified clathrin-coated membranes or a mixture of clathrin-coated and noncoated membranes. Electron micr…

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  • A potential cargo for HIP1 is huntingtin.

    “A potential cargo for HIP1 is huntingtin, which interacts with the N-terminal segment of HIP1 (Wanker et al., 1997) and has been localized to clathrin-coated structures and endosomes (Velier et al., 1998).”

    From Disabled‐2 exhibits the properties of a cargo‐selective endocytic clathrin adaptor (2002) · cites this paper as Velier et al., 1998

  • Huntingtin has been localized to clathrin-coated structures and endosomes.

    “A potential cargo for HIP1 is huntingtin, which interacts with the N-terminal segment of HIP1 (Wanker et al., 1997) and has been localized to clathrin-coated structures and endosomes (Velier et al., 1998).”

    From Disabled‐2 exhibits the properties of a cargo‐selective endocytic clathrin adaptor (2002) · cites this paper as Velier et al., 1998

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Research works printed but not linked: 38

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Metadata

Authors
Velier, J., Kim, M., Schwarz, C., Kim, T. W., Sapp, E., Chase, K., Aronin, N., & DiFiglia, M.
Venue
Experimental Neurology
Publisher
Elsevier BV
Published
1998-07
Volume
152
Issue
1
Pages
34-40
ISSN
0014-4886
DOI
10.1006/exnr.1998.6832
Cited by
258
References
1
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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