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Functional relevance of the interact...
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McGuire, John Russel.
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Functional relevance of the interaction between Huntingtin associated protein-1 and kinesin light chain.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
Functional relevance of the interaction between Huntingtin associated protein-1 and kinesin light chain./
作者:
McGuire, John Russel.
面頁冊數:
104 p.
附註:
Source: Dissertation Abstracts International, Volume: 67-03, Section: B, page: 1286.
Contained By:
Dissertation Abstracts International67-03B.
標題:
Biology, Molecular. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3212382
ISBN:
9780542614477
Functional relevance of the interaction between Huntingtin associated protein-1 and kinesin light chain.
McGuire, John Russel.
Functional relevance of the interaction between Huntingtin associated protein-1 and kinesin light chain.
- 104 p.
Source: Dissertation Abstracts International, Volume: 67-03, Section: B, page: 1286.
Thesis (Ph.D.)--Emory University, 2006.
Huntingtin associated protein-1 (HAP1) was initially identified as an interacting partner of huntingtin, the Huntington disease (HD) protein. Unlike huntingtin that is ubiquitously expressed throughout the brain and body, HAP1 is enriched in neurons, suggesting that its dysfunction could contribute to HD neuropathology. Growing evidence has demonstrated that HAP1 and huntingtin are anterogradely transported in axons and that the abnormal interaction between mutant huntingtin and HAP1 may impair axonal transport. However, the exact role of HAP1 in anterograde transport remains unclear. Here we report that HAP1 interacts with kinesin light chain (KLC), a subunit of the kinesin motor complex that drives anterograde transport along microtubules in neuronal processes. Biochemical and immunocytochemical data confirm the interaction which was originally shown in a yeast-2-hybrid screen. We also show that altering cellular levels of HAP1 has a significant effect on kinesin-dependent vesicle trafficking and neurite outgrowth. Finally, we demonstrate that expression of mutant huntingtin inhibits the transport of HAP1 from the cell body to the growth cone of neuronal cells. These studies provide a molecular basis for the participation of HAP1 in anterograde transport and suggest a possible mechanism by which mutant htt can disrupt kinesin-dependent transport.
ISBN: 9780542614477Subjects--Topical Terms:
1017719
Biology, Molecular.
Functional relevance of the interaction between Huntingtin associated protein-1 and kinesin light chain.
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Huntingtin associated protein-1 (HAP1) was initially identified as an interacting partner of huntingtin, the Huntington disease (HD) protein. Unlike huntingtin that is ubiquitously expressed throughout the brain and body, HAP1 is enriched in neurons, suggesting that its dysfunction could contribute to HD neuropathology. Growing evidence has demonstrated that HAP1 and huntingtin are anterogradely transported in axons and that the abnormal interaction between mutant huntingtin and HAP1 may impair axonal transport. However, the exact role of HAP1 in anterograde transport remains unclear. Here we report that HAP1 interacts with kinesin light chain (KLC), a subunit of the kinesin motor complex that drives anterograde transport along microtubules in neuronal processes. Biochemical and immunocytochemical data confirm the interaction which was originally shown in a yeast-2-hybrid screen. We also show that altering cellular levels of HAP1 has a significant effect on kinesin-dependent vesicle trafficking and neurite outgrowth. Finally, we demonstrate that expression of mutant huntingtin inhibits the transport of HAP1 from the cell body to the growth cone of neuronal cells. These studies provide a molecular basis for the participation of HAP1 in anterograde transport and suggest a possible mechanism by which mutant htt can disrupt kinesin-dependent transport.
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