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| | <StructureSection load='5c1f' size='340' side='right'caption='[[5c1f]], [[Resolution|resolution]] 2.36Å' scene=''> | | <StructureSection load='5c1f' size='340' side='right'caption='[[5c1f]], [[Resolution|resolution]] 2.36Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5c1f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C1F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C1F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5c1f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C1F FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">imp2, SPBC11C11.02 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</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=5c1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c1f OCA], [https://pdbe.org/5c1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c1f RCSB], [https://www.ebi.ac.uk/pdbsum/5c1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c1f ProSAT]</span></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=5c1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c1f OCA], [http://pdbe.org/5c1f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c1f RCSB], [http://www.ebi.ac.uk/pdbsum/5c1f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c1f ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IMP2_SCHPO IMP2_SCHPO]] Required for normal septation. Involved in the disassembly of the medial ring during septation.<ref>PMID:9786952</ref> | + | [https://www.uniprot.org/uniprot/IMP2_SCHPO IMP2_SCHPO] Required for normal septation. Involved in the disassembly of the medial ring during septation.<ref>PMID:9786952</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Fission yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kooi, C W.Vander]] | + | [[Category: Schizosaccharomyces pombe 972h-]] |
| - | [[Category: Cell cycle]] | + | [[Category: Vander Kooi CW]] |
| - | [[Category: Imp2 f-bar membrane binding]]
| + | |
| Structural highlights
Function
IMP2_SCHPO Required for normal septation. Involved in the disassembly of the medial ring during septation.[1]
Publication Abstract from PubMed
F-BAR proteins link cellular membranes to the actin cytoskeleton in many biological processes. Here we investigated the function of the Schizosaccharomyces pombe Imp2 F-BAR domain in cytokinesis and find that it is critical for Imp2's role in contractile ring constriction and disassembly. To understand mechanistically how the F-BAR domain functions, we determined its structure, elucidated how it interacts with membranes, and identified an interaction between dimers that allows helical oligomerization and membrane tubulation. Using mutations that block either membrane binding or tubulation, we find that membrane binding is required for Imp2's cytokinetic function but that oligomerization and tubulation, activities often deemed central to F-BAR protein function, are dispensable. Accordingly, F-BARs that do not have the capacity to tubulate membranes functionally substitute for the Imp2 F-BAR, establishing that its major role is as a cell-cycle-regulated bridge between the membrane and Imp2 protein partners, rather than as a driver of membrane curvature.
The Tubulation Activity of a Fission Yeast F-BAR Protein Is Dispensable for Its Function in Cytokinesis.,McDonald NA, Takizawa Y, Feoktistova A, Xu P, Ohi MD, Vander Kooi CW, Gould KL Cell Rep. 2016 Jan 13. pii: S2211-1247(15)01503-X. doi:, 10.1016/j.celrep.2015.12.062. PMID:26776521[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Demeter J, Sazer S. imp2, a new component of the actin ring in the fission yeast Schizosaccharomyces pombe. J Cell Biol. 1998 Oct 19;143(2):415-27. PMID:9786952
- ↑ McDonald NA, Takizawa Y, Feoktistova A, Xu P, Ohi MD, Vander Kooi CW, Gould KL. The Tubulation Activity of a Fission Yeast F-BAR Protein Is Dispensable for Its Function in Cytokinesis. Cell Rep. 2016 Jan 13. pii: S2211-1247(15)01503-X. doi:, 10.1016/j.celrep.2015.12.062. PMID:26776521 doi:http://dx.doi.org/10.1016/j.celrep.2015.12.062
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