File Download
Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1083/jcb.201603050
- Scopus: eid_2-s2.0-84971500608
- PMID: 27185835
- WOS: WOS:000376814800006
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: The structured core of human β tubulin confers isotype-specific polymerization properties
Title | The structured core of human β tubulin confers isotype-specific polymerization properties |
---|---|
Authors | |
Issue Date | 2016 |
Citation | Journal of Cell Biology, 2016, v. 213, n. 4, p. 425-433 How to Cite? |
Abstract | © 2016 Liu. Diversity in cytoskeleton organization and function may be achieved through variations in primary sequence of tubulin isotypes. Recently, isotype functional diversity has been linked to a "tubulin code" in which the C-terminal tail, a region of substantial sequence divergence between isotypes, specifies interactions with microtubule-associated proteins. However, it is not known whether residue changes in this region alter microtubule dynamic instability. Here, we examine recombinant tubulin with human β isotype IIB and characterize polymerization dynamics. Microtubules with βIIB have catastrophe frequencies approximately threefold lower than those with isotype βIII, a suppression similar to that achieved by regulatory proteins. Further, we generate chimeric β tubulins with native tail sequences swapped between isotypes. These chimeras have catastrophe frequencies similar to that of the corresponding full-length construct with the same core sequence. Together, our data indicate that residue changes within the conserved β tubulin core are largely responsible for the observed isotype-specific changes in dynamic instability parameters and tune tubulin's polymerization properties across a wide range. |
Persistent Identifier | http://hdl.handle.net/10722/277652 |
ISSN | 2023 Impact Factor: 7.4 2023 SCImago Journal Rankings: 3.717 |
ISI Accession Number ID |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Pamula, Melissa C. | - |
dc.contributor.author | Ti, Shih Chieh | - |
dc.contributor.author | Kapoor, Tarun M. | - |
dc.date.accessioned | 2019-09-27T08:29:36Z | - |
dc.date.available | 2019-09-27T08:29:36Z | - |
dc.date.issued | 2016 | - |
dc.identifier.citation | Journal of Cell Biology, 2016, v. 213, n. 4, p. 425-433 | - |
dc.identifier.issn | 0021-9525 | - |
dc.identifier.uri | http://hdl.handle.net/10722/277652 | - |
dc.description.abstract | © 2016 Liu. Diversity in cytoskeleton organization and function may be achieved through variations in primary sequence of tubulin isotypes. Recently, isotype functional diversity has been linked to a "tubulin code" in which the C-terminal tail, a region of substantial sequence divergence between isotypes, specifies interactions with microtubule-associated proteins. However, it is not known whether residue changes in this region alter microtubule dynamic instability. Here, we examine recombinant tubulin with human β isotype IIB and characterize polymerization dynamics. Microtubules with βIIB have catastrophe frequencies approximately threefold lower than those with isotype βIII, a suppression similar to that achieved by regulatory proteins. Further, we generate chimeric β tubulins with native tail sequences swapped between isotypes. These chimeras have catastrophe frequencies similar to that of the corresponding full-length construct with the same core sequence. Together, our data indicate that residue changes within the conserved β tubulin core are largely responsible for the observed isotype-specific changes in dynamic instability parameters and tune tubulin's polymerization properties across a wide range. | - |
dc.language | eng | - |
dc.relation.ispartof | Journal of Cell Biology | - |
dc.title | The structured core of human β tubulin confers isotype-specific polymerization properties | - |
dc.type | Article | - |
dc.description.nature | published_or_final_version | - |
dc.identifier.doi | 10.1083/jcb.201603050 | - |
dc.identifier.pmid | 27185835 | - |
dc.identifier.scopus | eid_2-s2.0-84971500608 | - |
dc.identifier.volume | 213 | - |
dc.identifier.issue | 4 | - |
dc.identifier.spage | 425 | - |
dc.identifier.epage | 433 | - |
dc.identifier.eissn | 1540-8140 | - |
dc.identifier.isi | WOS:000376814800006 | - |
dc.identifier.issnl | 0021-9525 | - |