Eintrag weiter verarbeiten
Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to Huntington's disease
Gespeichert in:
| Zeitschriftentitel: | Journal of Cell Science |
|---|---|
| Personen und Körperschaften: | , , |
| In: | Journal of Cell Science, 115, 2002, 5, S. 941-948 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
The Company of Biologists
|
| Schlagwörter: |
| author_facet |
Hoffner, Guylaine Kahlem, Pascal Djian, Philippe Hoffner, Guylaine Kahlem, Pascal Djian, Philippe |
|---|---|
| author |
Hoffner, Guylaine Kahlem, Pascal Djian, Philippe |
| spellingShingle |
Hoffner, Guylaine Kahlem, Pascal Djian, Philippe Journal of Cell Science Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to Huntington's disease Cell Biology |
| author_sort |
hoffner, guylaine |
| spelling |
Hoffner, Guylaine Kahlem, Pascal Djian, Philippe 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.115.5.941 <jats:p>Huntington's disease results from an expansion of a series of glutamine repeats in the protein huntingtin. We have discovered from immunopurification studies that huntingtin combines specifically with the β subunit of tubulin. This binding explains why huntingtin can be shown on assembled microtubules by electron microscopy. Immunostaining shows that most of the huntingtin in the cytoplasm is associated with microtubules. Huntingtin is particularly abundant in the perinuclear region, where it is also associated with microtubules and in the centrosomal region, where it co-localizes withγ-tubulin. In Huntington's disease, inclusions are often nuclear or perinuclear. Since the perinuclear concentration of huntingtin does not depend on the number of its glutamine repeats, we propose that inclusions are found in perinuclear and intranuclear locations because the β-tubulin binding property of huntingtin brings it to the perinuclear region, from which it readily gains access to the nucleus. The mutational glutamine expansion then promotes insolubility and results in an inclusion.</jats:p> Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to Huntington's disease Journal of Cell Science |
| doi_str_mv |
10.1242/jcs.115.5.941 |
| facet_avail |
Online Free |
| finc_class_facet |
Biologie |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTI0Mi9qY3MuMTE1LjUuOTQx |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTI0Mi9qY3MuMTE1LjUuOTQx |
| institution |
DE-15 DE-Pl11 DE-Rs1 DE-105 DE-14 DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-D161 DE-Zwi2 DE-Gla1 DE-Zi4 |
| imprint |
The Company of Biologists, 2002 |
| imprint_str_mv |
The Company of Biologists, 2002 |
| issn |
1477-9137 0021-9533 |
| issn_str_mv |
1477-9137 0021-9533 |
| language |
English |
| mega_collection |
The Company of Biologists (CrossRef) |
| match_str |
hoffner2002perinuclearlocalizationofhuntingtinasaconsequenceofitsbindingtomicrotubulesthroughaninteractionwithbtubulinrelevancetohuntingtonsdisease |
| publishDateSort |
2002 |
| publisher |
The Company of Biologists |
| recordtype |
ai |
| record_format |
ai |
| series |
Journal of Cell Science |
| source_id |
49 |
| title |
Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to Huntington's disease |
| title_unstemmed |
Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to Huntington's disease |
| title_full |
Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to Huntington's disease |
| title_fullStr |
Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to Huntington's disease |
| title_full_unstemmed |
Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to Huntington's disease |
| title_short |
Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to Huntington's disease |
| title_sort |
perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to huntington's disease |
| topic |
Cell Biology |
| url |
http://dx.doi.org/10.1242/jcs.115.5.941 |
| publishDate |
2002 |
| physical |
941-948 |
| description |
<jats:p>Huntington's disease results from an expansion of a series of glutamine repeats in the protein huntingtin. We have discovered from immunopurification studies that huntingtin combines specifically with the β subunit of tubulin. This binding explains why huntingtin can be shown on assembled microtubules by electron microscopy. Immunostaining shows that most of the huntingtin in the cytoplasm is associated with microtubules. Huntingtin is particularly abundant in the perinuclear region, where it is also associated with microtubules and in the centrosomal region, where it co-localizes withγ-tubulin. In Huntington's disease, inclusions are often nuclear or perinuclear. Since the perinuclear concentration of huntingtin does not depend on the number of its glutamine repeats, we propose that inclusions are found in perinuclear and intranuclear locations because the β-tubulin binding property of huntingtin brings it to the perinuclear region, from which it readily gains access to the nucleus. The mutational glutamine expansion then promotes insolubility and results in an inclusion.</jats:p> |
| container_issue |
5 |
| container_start_page |
941 |
| container_title |
Journal of Cell Science |
| container_volume |
115 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792340316603285512 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T16:01:02.553Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Perinuclear+localization+of+huntingtin+as+a+consequence+of+its+binding+to+microtubules+through+an+interaction+with+%CE%B2-tubulin%3A+relevance+to+Huntington%27s+disease&rft.date=2002-03-01&genre=article&issn=0021-9533&volume=115&issue=5&spage=941&epage=948&pages=941-948&jtitle=Journal+of+Cell+Science&atitle=Perinuclear+localization+of+huntingtin+as+a+consequence+of+its+binding+to+microtubules+through+an+interaction+with+%CE%B2-tubulin%3A+relevance+to+Huntington%27s+disease&aulast=Djian&aufirst=Philippe&rft_id=info%3Adoi%2F10.1242%2Fjcs.115.5.941&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792340316603285512 |
| author | Hoffner, Guylaine, Kahlem, Pascal, Djian, Philippe |
| author_facet | Hoffner, Guylaine, Kahlem, Pascal, Djian, Philippe, Hoffner, Guylaine, Kahlem, Pascal, Djian, Philippe |
| author_sort | hoffner, guylaine |
| container_issue | 5 |
| container_start_page | 941 |
| container_title | Journal of Cell Science |
| container_volume | 115 |
| description | <jats:p>Huntington's disease results from an expansion of a series of glutamine repeats in the protein huntingtin. We have discovered from immunopurification studies that huntingtin combines specifically with the β subunit of tubulin. This binding explains why huntingtin can be shown on assembled microtubules by electron microscopy. Immunostaining shows that most of the huntingtin in the cytoplasm is associated with microtubules. Huntingtin is particularly abundant in the perinuclear region, where it is also associated with microtubules and in the centrosomal region, where it co-localizes withγ-tubulin. In Huntington's disease, inclusions are often nuclear or perinuclear. Since the perinuclear concentration of huntingtin does not depend on the number of its glutamine repeats, we propose that inclusions are found in perinuclear and intranuclear locations because the β-tubulin binding property of huntingtin brings it to the perinuclear region, from which it readily gains access to the nucleus. The mutational glutamine expansion then promotes insolubility and results in an inclusion.</jats:p> |
| doi_str_mv | 10.1242/jcs.115.5.941 |
| facet_avail | Online, Free |
| finc_class_facet | Biologie |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTI0Mi9qY3MuMTE1LjUuOTQx |
| imprint | The Company of Biologists, 2002 |
| imprint_str_mv | The Company of Biologists, 2002 |
| institution | DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-D161, DE-Zwi2, DE-Gla1, DE-Zi4 |
| issn | 1477-9137, 0021-9533 |
| issn_str_mv | 1477-9137, 0021-9533 |
| language | English |
| last_indexed | 2024-03-01T16:01:02.553Z |
| match_str | hoffner2002perinuclearlocalizationofhuntingtinasaconsequenceofitsbindingtomicrotubulesthroughaninteractionwithbtubulinrelevancetohuntingtonsdisease |
| mega_collection | The Company of Biologists (CrossRef) |
| physical | 941-948 |
| publishDate | 2002 |
| publishDateSort | 2002 |
| publisher | The Company of Biologists |
| record_format | ai |
| recordtype | ai |
| series | Journal of Cell Science |
| source_id | 49 |
| spelling | Hoffner, Guylaine Kahlem, Pascal Djian, Philippe 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.115.5.941 <jats:p>Huntington's disease results from an expansion of a series of glutamine repeats in the protein huntingtin. We have discovered from immunopurification studies that huntingtin combines specifically with the β subunit of tubulin. This binding explains why huntingtin can be shown on assembled microtubules by electron microscopy. Immunostaining shows that most of the huntingtin in the cytoplasm is associated with microtubules. Huntingtin is particularly abundant in the perinuclear region, where it is also associated with microtubules and in the centrosomal region, where it co-localizes withγ-tubulin. In Huntington's disease, inclusions are often nuclear or perinuclear. Since the perinuclear concentration of huntingtin does not depend on the number of its glutamine repeats, we propose that inclusions are found in perinuclear and intranuclear locations because the β-tubulin binding property of huntingtin brings it to the perinuclear region, from which it readily gains access to the nucleus. The mutational glutamine expansion then promotes insolubility and results in an inclusion.</jats:p> Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to Huntington's disease Journal of Cell Science |
| spellingShingle | Hoffner, Guylaine, Kahlem, Pascal, Djian, Philippe, Journal of Cell Science, Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to Huntington's disease, Cell Biology |
| title | Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to Huntington's disease |
| title_full | Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to Huntington's disease |
| title_fullStr | Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to Huntington's disease |
| title_full_unstemmed | Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to Huntington's disease |
| title_short | Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to Huntington's disease |
| title_sort | perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to huntington's disease |
| title_unstemmed | Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: relevance to Huntington's disease |
| topic | Cell Biology |
| url | http://dx.doi.org/10.1242/jcs.115.5.941 |