8cx6: Difference between revisions
New page: '''Unreleased structure''' The entry 8cx6 is ON HOLD Authors: Guo, C., Alfaro-Aco, R., Russell, R., Zhang, C., Petry, S., Polenova, T. Description: TPX2 Minimal Active Domain on Microt... |
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The | ==TPX2 Minimal Active Domain on Microtubules== | ||
<StructureSection load='8cx6' size='340' side='right'caption='[[8cx6]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8cx6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CX6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CX6 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8cx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cx6 OCA], [https://pdbe.org/8cx6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cx6 RCSB], [https://www.ebi.ac.uk/pdbsum/8cx6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cx6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TPX2A_XENLA TPX2A_XENLA] Spindle assembly factor. Required for normal assembly of mitotic spindles. Mediates the binding kif15 and aurka to spindle microtubules. Required for targeting kif15 to microtubule minus ends. Activates aurka by promoting its autophosphorylation and protects the phosphorylated residue against dephosphorylation (By similarity).<ref>PMID:10871281</ref> <ref>PMID:19556869</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Targeting protein for Xklp2 (TPX2) is a key factor that stimulates branching microtubule nucleation during cell division. Upon binding to microtubules (MTs), TPX2 forms condensates via liquid-liquid phase separation, which facilitates recruitment of microtubule nucleation factors and tubulin. We report the structure of the TPX2 C-terminal minimal active domain (TPX2(alpha5-alpha7)) on the microtubule lattice determined by magic-angle-spinning NMR. We demonstrate that TPX2(alpha5-alpha7) forms a co-condensate with soluble tubulin on microtubules and binds to MTs between two adjacent protofilaments and at the intersection of four tubulin heterodimers. These interactions stabilize the microtubules and promote the recruitment of tubulin. Our results reveal that TPX2(alpha5-alpha7) is disordered in solution and adopts a folded structure on MTs, indicating that TPX2(alpha5-alpha7) undergoes structural changes from unfolded to folded states upon binding to microtubules. The aromatic residues form dense interactions in the core, which stabilize folding of TPX2(alpha5-alpha7) on microtubules. This work informs on how the phase-separated TPX2(alpha5-alpha7) behaves on microtubules and represents an atomic-level structural characterization of a protein that is involved in a condensate on cytoskeletal filaments. | |||
Structural basis of protein condensation on microtubules underlying branching microtubule nucleation.,Guo C, Alfaro-Aco R, Zhang C, Russell RW, Petry S, Polenova T Nat Commun. 2023 Jun 21;14(1):3682. doi: 10.1038/s41467-023-39176-z. PMID:37344496<ref>PMID:37344496</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8cx6" style="background-color:#fffaf0;"></div> | ||
[[Category: Guo | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Xenopus laevis]] | |||
[[Category: Alfaro-Aco R]] | |||
[[Category: Guo C]] | |||
[[Category: Petry S]] | |||
[[Category: Polenova T]] | |||
[[Category: Russell R]] | |||
[[Category: Zhang C]] | |||
Latest revision as of 00:15, 29 June 2023
TPX2 Minimal Active Domain on MicrotubulesTPX2 Minimal Active Domain on Microtubules
Structural highlights
FunctionTPX2A_XENLA Spindle assembly factor. Required for normal assembly of mitotic spindles. Mediates the binding kif15 and aurka to spindle microtubules. Required for targeting kif15 to microtubule minus ends. Activates aurka by promoting its autophosphorylation and protects the phosphorylated residue against dephosphorylation (By similarity).[1] [2] Publication Abstract from PubMedTargeting protein for Xklp2 (TPX2) is a key factor that stimulates branching microtubule nucleation during cell division. Upon binding to microtubules (MTs), TPX2 forms condensates via liquid-liquid phase separation, which facilitates recruitment of microtubule nucleation factors and tubulin. We report the structure of the TPX2 C-terminal minimal active domain (TPX2(alpha5-alpha7)) on the microtubule lattice determined by magic-angle-spinning NMR. We demonstrate that TPX2(alpha5-alpha7) forms a co-condensate with soluble tubulin on microtubules and binds to MTs between two adjacent protofilaments and at the intersection of four tubulin heterodimers. These interactions stabilize the microtubules and promote the recruitment of tubulin. Our results reveal that TPX2(alpha5-alpha7) is disordered in solution and adopts a folded structure on MTs, indicating that TPX2(alpha5-alpha7) undergoes structural changes from unfolded to folded states upon binding to microtubules. The aromatic residues form dense interactions in the core, which stabilize folding of TPX2(alpha5-alpha7) on microtubules. This work informs on how the phase-separated TPX2(alpha5-alpha7) behaves on microtubules and represents an atomic-level structural characterization of a protein that is involved in a condensate on cytoskeletal filaments. Structural basis of protein condensation on microtubules underlying branching microtubule nucleation.,Guo C, Alfaro-Aco R, Zhang C, Russell RW, Petry S, Polenova T Nat Commun. 2023 Jun 21;14(1):3682. doi: 10.1038/s41467-023-39176-z. PMID:37344496[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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