The Aspergillus nidulans kinesin-3 tail is necessary and sufficient to recognize modified microtubules.
Posttranslational microtubule modifications (PTMs) are numerous; however, the biochemical and cell biological roles of those modifications remain mostly an enigma. The Aspergillus nidulans kinesin-3 UncA uses preferably modified microtubules (MTs) as tracks for vesicle transportation. Here, we show...
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2012
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oai:doaj.org-article:96fd0b9d436b4c5b8a458d6f326487c62021-11-18T07:27:34ZThe Aspergillus nidulans kinesin-3 tail is necessary and sufficient to recognize modified microtubules.1932-620310.1371/journal.pone.0030976https://doaj.org/article/96fd0b9d436b4c5b8a458d6f326487c62012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22363525/?tool=EBIhttps://doaj.org/toc/1932-6203Posttranslational microtubule modifications (PTMs) are numerous; however, the biochemical and cell biological roles of those modifications remain mostly an enigma. The Aspergillus nidulans kinesin-3 UncA uses preferably modified microtubules (MTs) as tracks for vesicle transportation. Here, we show that a positively charged region in the tail of UncA (amino acids 1316 to 1402) is necessary for the recognition of modified MTs. Chimeric proteins composed of the kinesin-1 motor domain and the UncA tail displayed the same specificity as UncA, suggesting that the UncA tail is sufficient to establish specificity. Interaction between the UncA tail and alpha-tubulin was shown using a yeast two-hybrid assay and in A. nidulans by bimolecular fluorescence complementation. This is the first demonstration of how a kinesin-3 motor protein distinguishes among different MT populations in fungal cells, and how specificity determination depends on the tail rather than the motor domain, as has been demonstrated for kinesin 1 in neuronal cells.Constanze SeidelNadine ZekertReinhard FischerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 2, p e30976 (2012) |
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Medicine R Science Q Constanze Seidel Nadine Zekert Reinhard Fischer The Aspergillus nidulans kinesin-3 tail is necessary and sufficient to recognize modified microtubules. |
description |
Posttranslational microtubule modifications (PTMs) are numerous; however, the biochemical and cell biological roles of those modifications remain mostly an enigma. The Aspergillus nidulans kinesin-3 UncA uses preferably modified microtubules (MTs) as tracks for vesicle transportation. Here, we show that a positively charged region in the tail of UncA (amino acids 1316 to 1402) is necessary for the recognition of modified MTs. Chimeric proteins composed of the kinesin-1 motor domain and the UncA tail displayed the same specificity as UncA, suggesting that the UncA tail is sufficient to establish specificity. Interaction between the UncA tail and alpha-tubulin was shown using a yeast two-hybrid assay and in A. nidulans by bimolecular fluorescence complementation. This is the first demonstration of how a kinesin-3 motor protein distinguishes among different MT populations in fungal cells, and how specificity determination depends on the tail rather than the motor domain, as has been demonstrated for kinesin 1 in neuronal cells. |
format |
article |
author |
Constanze Seidel Nadine Zekert Reinhard Fischer |
author_facet |
Constanze Seidel Nadine Zekert Reinhard Fischer |
author_sort |
Constanze Seidel |
title |
The Aspergillus nidulans kinesin-3 tail is necessary and sufficient to recognize modified microtubules. |
title_short |
The Aspergillus nidulans kinesin-3 tail is necessary and sufficient to recognize modified microtubules. |
title_full |
The Aspergillus nidulans kinesin-3 tail is necessary and sufficient to recognize modified microtubules. |
title_fullStr |
The Aspergillus nidulans kinesin-3 tail is necessary and sufficient to recognize modified microtubules. |
title_full_unstemmed |
The Aspergillus nidulans kinesin-3 tail is necessary and sufficient to recognize modified microtubules. |
title_sort |
aspergillus nidulans kinesin-3 tail is necessary and sufficient to recognize modified microtubules. |
publisher |
Public Library of Science (PLoS) |
publishDate |
2012 |
url |
https://doaj.org/article/96fd0b9d436b4c5b8a458d6f326487c6 |
work_keys_str_mv |
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