File Download
There are no files associated with this item.
Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1073/pnas.1609903113
- Scopus: eid_2-s2.0-84983657268
- PMID: 27493215
- WOS: WOS:000381860800034
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: Near-atomic cryo-EM structure of PRC1 bound to the microtubule
Title | Near-atomic cryo-EM structure of PRC1 bound to the microtubule |
---|---|
Authors | |
Keywords | Microtubules MAPs Cytoskeleton Cryo-EM PRC1 |
Issue Date | 2016 |
Citation | Proceedings of the National Academy of Sciences of the United States of America, 2016, v. 113, n. 34, p. 9430-9439 How to Cite? |
Abstract | © 2016, National Academy of Sciences. All rights reserved. Proteins that associate with microtubules (MTs) are crucial to generate MT arrays and establish different cellular architectures. One example is PRC1 (protein regulator of cytokinesis 1), which cross-links antiparallel MTs and is essential for the completion of mitosis and cytokinesis. Here we describe a 4-Å-resolution cryo-EM structure of monomeric PRC1 bound to MTs. Residues in the spectrin domain of PRC1 contacting the MT are highly conserved and interact with the same pocket recognized by kinesin. We additionally found that PRC1 promotes MT assembly even in the presence of the MT stabilizer taxol. Interestingly, the angle of the spectrin domain on the MT surface corresponds to the previously observed cross-bridge angle between MTs cross-linked by full-length, dimeric PRC1. This finding, together with molecular dynamic simulations describing the intrinsic flexibility of PRC1, suggests that the MT-spectrin domain interface determines the geometry of the MT arrays cross-linked by PRC1. |
Persistent Identifier | http://hdl.handle.net/10722/277656 |
ISSN | 2023 Impact Factor: 9.4 2023 SCImago Journal Rankings: 3.737 |
ISI Accession Number ID |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kellogg, Elizabeth H. | - |
dc.contributor.author | Howes, Stuart | - |
dc.contributor.author | Ti, Shih Chieh | - |
dc.contributor.author | Ramírez-Aportela, Erney | - |
dc.contributor.author | Kapoor, Tarun M. | - |
dc.contributor.author | Chacón, Pablo | - |
dc.contributor.author | Nogales, Eva | - |
dc.date.accessioned | 2019-09-27T08:29:36Z | - |
dc.date.available | 2019-09-27T08:29:36Z | - |
dc.date.issued | 2016 | - |
dc.identifier.citation | Proceedings of the National Academy of Sciences of the United States of America, 2016, v. 113, n. 34, p. 9430-9439 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.uri | http://hdl.handle.net/10722/277656 | - |
dc.description.abstract | © 2016, National Academy of Sciences. All rights reserved. Proteins that associate with microtubules (MTs) are crucial to generate MT arrays and establish different cellular architectures. One example is PRC1 (protein regulator of cytokinesis 1), which cross-links antiparallel MTs and is essential for the completion of mitosis and cytokinesis. Here we describe a 4-Å-resolution cryo-EM structure of monomeric PRC1 bound to MTs. Residues in the spectrin domain of PRC1 contacting the MT are highly conserved and interact with the same pocket recognized by kinesin. We additionally found that PRC1 promotes MT assembly even in the presence of the MT stabilizer taxol. Interestingly, the angle of the spectrin domain on the MT surface corresponds to the previously observed cross-bridge angle between MTs cross-linked by full-length, dimeric PRC1. This finding, together with molecular dynamic simulations describing the intrinsic flexibility of PRC1, suggests that the MT-spectrin domain interface determines the geometry of the MT arrays cross-linked by PRC1. | - |
dc.language | eng | - |
dc.relation.ispartof | Proceedings of the National Academy of Sciences of the United States of America | - |
dc.subject | Microtubules | - |
dc.subject | MAPs | - |
dc.subject | Cytoskeleton | - |
dc.subject | Cryo-EM | - |
dc.subject | PRC1 | - |
dc.title | Near-atomic cryo-EM structure of PRC1 bound to the microtubule | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1073/pnas.1609903113 | - |
dc.identifier.pmid | 27493215 | - |
dc.identifier.pmid | 27493215 | - |
dc.identifier.scopus | eid_2-s2.0-84983657268 | - |
dc.identifier.volume | 113 | - |
dc.identifier.issue | 34 | - |
dc.identifier.spage | 9430 | - |
dc.identifier.epage | 9439 | - |
dc.identifier.eissn | 1091-6490 | - |
dc.identifier.isi | WOS:000381860800034 | - |
dc.identifier.issnl | 0027-8424 | - |