6abr

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'''Unreleased structure'''
 
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The entry 6abr is ON HOLD until Paper Publication
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==Actin interacting protein 5 (Aip5, wild type)==
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<StructureSection load='6abr' size='340' side='right'caption='[[6abr]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6abr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ABR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ABR FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6abr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6abr OCA], [http://pdbe.org/6abr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6abr RCSB], [http://www.ebi.ac.uk/pdbsum/6abr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6abr ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A multiprotein complex polarisome nucleates actin cables for polarized cell growth in budding yeast and filamentous fungi. However, the dynamic regulations of polarisome proteins in polymerizing actin under physiological and stress conditions remains unknown. We identify a previously functionally unknown polarisome member, actin-interacting-protein 5 (Aip5), which promotes actin assembly synergistically with formin Bni1. Aip5-C terminus is responsible for its activities by interacting with G-actin and Bni1. Through N-terminal intrinsically disordered region, Aip5 forms high-order oligomers and generate cytoplasmic condensates under the stresses conditions. The molecular dynamics and reversibility of Aip5 condensates are regulated by scaffolding protein Spa2 via liquid-liquid phase separation both in vitro and in vivo. In the absence of Spa2, Aip5 condensates hamper cell growth and actin cable structures under stress treatment. The present study reveals the mechanisms of actin assembly for polarity establishment and the adaptation in stress conditions to protect actin assembly by protein phase separation.
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Authors:
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Polarisome scaffolder Spa2-mediated macromolecular condensation of Aip5 for actin polymerization.,Xie Y, Sun J, Han X, Tursic-Wunder A, Toh JDW, Hong W, Gao YG, Miao Y Nat Commun. 2019 Nov 7;10(1):5078. doi: 10.1038/s41467-019-13125-1. PMID:31699995<ref>PMID:31699995</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6abr" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Gao, Y G]]
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[[Category: Hong, W]]
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[[Category: MIao, Y]]
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[[Category: Sun, J]]
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[[Category: Toh, J D.W]]
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[[Category: Xie, Y]]
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[[Category: Structural protein]]

Revision as of 15:15, 20 November 2019

Actin interacting protein 5 (Aip5, wild type)

PDB ID 6abr

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