Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro.
Kinesin-1 plays a major role in anterograde transport of intracellular cargo along microtubules. Currently, there is an ongoing debate of whether α-tubulin K40 acetylation directly enhances the velocity of kinesin-1 and its affinity to the microtubule track. We compared motor motility on microtubule...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2012-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3411631?pdf=render |
| _version_ | 1818619891234635776 |
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| author | Wilhelm J Walter Václav Beránek Elisabeth Fischermeier Stefan Diez |
| author_facet | Wilhelm J Walter Václav Beránek Elisabeth Fischermeier Stefan Diez |
| author_sort | Wilhelm J Walter |
| collection | DOAJ |
| description | Kinesin-1 plays a major role in anterograde transport of intracellular cargo along microtubules. Currently, there is an ongoing debate of whether α-tubulin K40 acetylation directly enhances the velocity of kinesin-1 and its affinity to the microtubule track. We compared motor motility on microtubules reconstituted from acetylated and deacetylated tubulin. For both, single- and multi-motor in vitro motility assays, we demonstrate that tubulin acetylation alone does not affect kinesin-1 velocity and run length. |
| first_indexed | 2024-12-16T17:44:41Z |
| format | Article |
| id | doaj.art-c9c29baf58f8453b899fd4065310e855 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-16T17:44:41Z |
| publishDate | 2012-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-c9c29baf58f8453b899fd4065310e8552022-12-21T22:22:30ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-0178e4221810.1371/journal.pone.0042218Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro.Wilhelm J WalterVáclav BeránekElisabeth FischermeierStefan DiezKinesin-1 plays a major role in anterograde transport of intracellular cargo along microtubules. Currently, there is an ongoing debate of whether α-tubulin K40 acetylation directly enhances the velocity of kinesin-1 and its affinity to the microtubule track. We compared motor motility on microtubules reconstituted from acetylated and deacetylated tubulin. For both, single- and multi-motor in vitro motility assays, we demonstrate that tubulin acetylation alone does not affect kinesin-1 velocity and run length.http://europepmc.org/articles/PMC3411631?pdf=render |
| spellingShingle | Wilhelm J Walter Václav Beránek Elisabeth Fischermeier Stefan Diez Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro. PLoS ONE |
| title | Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro. |
| title_full | Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro. |
| title_fullStr | Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro. |
| title_full_unstemmed | Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro. |
| title_short | Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro. |
| title_sort | tubulin acetylation alone does not affect kinesin 1 velocity and run length in vitro |
| url | http://europepmc.org/articles/PMC3411631?pdf=render |
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