6lag: Difference between revisions
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==Solution structure of SPA-2 SHD== | ==Solution structure of SPA-2 SHD== | ||
<StructureSection load='6lag' size='340' side='right'caption='[[6lag]]' scene=''> | <StructureSection load='6lag' size='340' side='right'caption='[[6lag]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full | <table><tr><td colspan='2'>[[6lag]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chrysonilia_crassa Chrysonilia crassa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LAG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LAG FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6lag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lag OCA], [http://pdbe.org/6lag PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lag RCSB], [http://www.ebi.ac.uk/pdbsum/6lag PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lag ProSAT]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spa2, NCU03115 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5141 Chrysonilia crassa])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6lag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lag OCA], [http://pdbe.org/6lag PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lag RCSB], [http://www.ebi.ac.uk/pdbsum/6lag PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lag ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Spitzenkorper (SPK) constitutes a collection of secretory vesicles and polarity-related proteins intimately associated with polarized growth of fungal hyphae. Many SPK-localized proteins are known, but their assembly and dynamics remain poorly understood. Here, we identify protein-protein interaction cascades leading to assembly of two SPK scaffolds and recruitment of diverse effectors in Neurospora crassa. Both scaffolds are transported to the SPK by the myosin V motor (MYO-5), with the coiled-coil protein SPZ-1 acting as cargo adaptor. Neither scaffold appears to be required for accumulation of SPK secretory vesicles. One scaffold consists of Leashin-2 (LAH-2), which is required for SPK localization of the signalling kinase COT-1 and the glycolysis enzyme GPI-1. The other scaffold comprises a complex of Janus-1 (JNS-1) and the polarisome protein SPA-2. Via its Spa homology domain (SHD), SPA-2 recruits a calponin domain-containing F-actin effector (CCP-1). The SHD NMR structure reveals a conserved surface groove required for effector binding. Similarities between SPA-2/JNS-1 and the metazoan GIT/PIX complex identify foundational features of the cell polarity apparatus that predate the fungal-metazoan divergence. | |||
Spitzenkorper assembly mechanisms reveal conserved features of fungal and metazoan polarity scaffolds.,Zheng P, Nguyen TA, Wong JY, Lee M, Nguyen TA, Fan JS, Yang D, Jedd G Nat Commun. 2020 Jun 5;11(1):2830. doi: 10.1038/s41467-020-16712-9. PMID:32503980<ref>PMID:32503980</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6lag" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Chrysonilia crassa]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fan | [[Category: Fan, J S]] | ||
[[Category: Jedd G]] | [[Category: Jedd, G]] | ||
[[Category: Wong | [[Category: Wong, J Y]] | ||
[[Category: Yang D]] | [[Category: Yang, D]] | ||
[[Category: Zheng P]] | [[Category: Zheng, P]] | ||
[[Category: Git-pix]] | |||
[[Category: Polarity]] | |||
[[Category: Shd]] | |||
[[Category: Signaling protein]] | |||
[[Category: Spa-2]] | |||
Revision as of 11:06, 11 November 2020
Solution structure of SPA-2 SHDSolution structure of SPA-2 SHD
Structural highlights
Publication Abstract from PubMedThe Spitzenkorper (SPK) constitutes a collection of secretory vesicles and polarity-related proteins intimately associated with polarized growth of fungal hyphae. Many SPK-localized proteins are known, but their assembly and dynamics remain poorly understood. Here, we identify protein-protein interaction cascades leading to assembly of two SPK scaffolds and recruitment of diverse effectors in Neurospora crassa. Both scaffolds are transported to the SPK by the myosin V motor (MYO-5), with the coiled-coil protein SPZ-1 acting as cargo adaptor. Neither scaffold appears to be required for accumulation of SPK secretory vesicles. One scaffold consists of Leashin-2 (LAH-2), which is required for SPK localization of the signalling kinase COT-1 and the glycolysis enzyme GPI-1. The other scaffold comprises a complex of Janus-1 (JNS-1) and the polarisome protein SPA-2. Via its Spa homology domain (SHD), SPA-2 recruits a calponin domain-containing F-actin effector (CCP-1). The SHD NMR structure reveals a conserved surface groove required for effector binding. Similarities between SPA-2/JNS-1 and the metazoan GIT/PIX complex identify foundational features of the cell polarity apparatus that predate the fungal-metazoan divergence. Spitzenkorper assembly mechanisms reveal conserved features of fungal and metazoan polarity scaffolds.,Zheng P, Nguyen TA, Wong JY, Lee M, Nguyen TA, Fan JS, Yang D, Jedd G Nat Commun. 2020 Jun 5;11(1):2830. doi: 10.1038/s41467-020-16712-9. PMID:32503980[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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