Microtubule minus-end stability is dictated by the tubulin off-rate
Dynamic organization of microtubule minus ends is vital for the formation and maintenance of acentrosomal microtubule arrays. In vitro, both microtubule ends switch between phases of assembly and disassembly, a behavior called dynamic instability. Although minus ends grow slower, their lifetimes are...
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| Veröffentlicht in: | The Journal of cell biology 2019-09, Vol.218 (9), p.2841-2853 |
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| container_title | The Journal of cell biology |
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| creator | Strothman, Claire Farmer, Veronica Arpağ, Göker Rodgers, Nicole Podolski, Marija Norris, Stephen Ohi, Ryoma Zanic, Marija |
| description | Dynamic organization of microtubule minus ends is vital for the formation and maintenance of acentrosomal microtubule arrays. In vitro, both microtubule ends switch between phases of assembly and disassembly, a behavior called dynamic instability. Although minus ends grow slower, their lifetimes are similar to those of plus ends. The mechanisms underlying these distinct dynamics remain unknown. Here, we use an in vitro reconstitution approach to investigate minus-end dynamics. We find that minus-end lifetimes are not defined by the mean size of the protective GTP-tubulin cap. Rather, we conclude that the distinct tubulin off-rate is the primary determinant of the difference between plus- and minus-end dynamics. Further, our results show that the minus-end-directed kinesin-14 HSET/KIFC1 suppresses tubulin off-rate to specifically suppress minus-end catastrophe. HSET maintains its protective minus-end activity even when challenged by a known microtubule depolymerase, kinesin-13 MCAK. Our results provide novel insight into the mechanisms of minus-end dynamics, essential for our understanding of microtubule minus-end regulation in cells. |
| doi_str_mv | 10.1083/jcb.201905019 |
| format | Article |
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In vitro, both microtubule ends switch between phases of assembly and disassembly, a behavior called dynamic instability. Although minus ends grow slower, their lifetimes are similar to those of plus ends. The mechanisms underlying these distinct dynamics remain unknown. Here, we use an in vitro reconstitution approach to investigate minus-end dynamics. We find that minus-end lifetimes are not defined by the mean size of the protective GTP-tubulin cap. Rather, we conclude that the distinct tubulin off-rate is the primary determinant of the difference between plus- and minus-end dynamics. Further, our results show that the minus-end-directed kinesin-14 HSET/KIFC1 suppresses tubulin off-rate to specifically suppress minus-end catastrophe. HSET maintains its protective minus-end activity even when challenged by a known microtubule depolymerase, kinesin-13 MCAK. Our results provide novel insight into the mechanisms of minus-end dynamics, essential for our understanding of microtubule minus-end regulation in cells.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.201905019</identifier><identifier>PMID: 31420452</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Animals ; Cattle ; Dismantling ; Dynamic stability ; Dynamics ; Guanosine triphosphate ; Kinesin ; Kinesins - chemistry ; Kinesins - metabolism ; Microtubules - chemistry ; Microtubules - metabolism ; Tubulin ; Tubulin - chemistry ; Tubulin - metabolism</subject><ispartof>The Journal of cell biology, 2019-09, Vol.218 (9), p.2841-2853</ispartof><rights>2019 Strothman et al.</rights><rights>Copyright Rockefeller University Press Sep 2019</rights><rights>2019 Strothman et al. 2019</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c415t-72966f039746f4d2528368c2d418b456f2b3a50454d21c9575efaa16bfec901b3</citedby><cites>FETCH-LOGICAL-c415t-72966f039746f4d2528368c2d418b456f2b3a50454d21c9575efaa16bfec901b3</cites><orcidid>0000-0002-5127-5819 ; 0000-0003-2711-9581 ; 0000-0001-7849-0626 ; 0000-0002-6893-2678</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31420452$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Strothman, Claire</creatorcontrib><creatorcontrib>Farmer, Veronica</creatorcontrib><creatorcontrib>Arpağ, Göker</creatorcontrib><creatorcontrib>Rodgers, Nicole</creatorcontrib><creatorcontrib>Podolski, Marija</creatorcontrib><creatorcontrib>Norris, Stephen</creatorcontrib><creatorcontrib>Ohi, Ryoma</creatorcontrib><creatorcontrib>Zanic, Marija</creatorcontrib><title>Microtubule minus-end stability is dictated by the tubulin off-rate</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Dynamic organization of microtubule minus ends is vital for the formation and maintenance of acentrosomal microtubule arrays. 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Our results provide novel insight into the mechanisms of minus-end dynamics, essential for our understanding of microtubule minus-end regulation in cells.</description><subject>Animals</subject><subject>Cattle</subject><subject>Dismantling</subject><subject>Dynamic stability</subject><subject>Dynamics</subject><subject>Guanosine triphosphate</subject><subject>Kinesin</subject><subject>Kinesins - chemistry</subject><subject>Kinesins - metabolism</subject><subject>Microtubules - chemistry</subject><subject>Microtubules - metabolism</subject><subject>Tubulin</subject><subject>Tubulin - chemistry</subject><subject>Tubulin - metabolism</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkUtLAzEUhYMotlaXbiXgxs3ozWseG0GKL6i40XVIMolNmc7USUbovzfaWtTNvYvzcTj3HoROCVwSKNnVwuhLCqQCkcYeGhPBISsJh300BqAkqwQVI3QUwgIAeMHZIRoxwilwQcdo-uRN38VBD43FS98OIbNtjUNU2jc-rrEPuPYmqmhrrNc4zi3-pn2LO-eyPgnH6MCpJtiT7Z6g17vbl-lDNnu-f5zezDLDiYhZQas8d8CqgueO11TQkuWloTUnpeYid1QzJVKspBFTiUJYpxTJtbOmAqLZBF1vfFeDXtra2Db2qpGr3i9Vv5ad8vKv0vq5fOs-ZF6QiueQDC62Bn33PtgQ5dIHY5tGtbYbgqS0ELTgIIqEnv9DF93Qt-m8RJUspasYTVS2odIPQ-it24UhIL_qkakeuasn8We_L9jRP32wT5Miik8</recordid><startdate>20190902</startdate><enddate>20190902</enddate><creator>Strothman, Claire</creator><creator>Farmer, Veronica</creator><creator>Arpağ, Göker</creator><creator>Rodgers, Nicole</creator><creator>Podolski, Marija</creator><creator>Norris, Stephen</creator><creator>Ohi, Ryoma</creator><creator>Zanic, Marija</creator><general>Rockefeller University Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-5127-5819</orcidid><orcidid>https://orcid.org/0000-0003-2711-9581</orcidid><orcidid>https://orcid.org/0000-0001-7849-0626</orcidid><orcidid>https://orcid.org/0000-0002-6893-2678</orcidid></search><sort><creationdate>20190902</creationdate><title>Microtubule minus-end stability is dictated by the tubulin off-rate</title><author>Strothman, Claire ; 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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Cattle Dismantling Dynamic stability Dynamics Guanosine triphosphate Kinesin Kinesins - chemistry Kinesins - metabolism Microtubules - chemistry Microtubules - metabolism Tubulin Tubulin - chemistry Tubulin - metabolism |
| title | Microtubule minus-end stability is dictated by the tubulin off-rate |
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