|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <SX load='5h3d' size='340' side='right' viewer='molstar' caption='[[5h3d]], [[Resolution|resolution]] 14.00Å' scene=''> | | <SX load='5h3d' size='340' side='right' viewer='molstar' caption='[[5h3d]], [[Resolution|resolution]] 14.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5h3d]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H3D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5H3D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5h3d]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H3D FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ckg|4ckg]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 14Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACAP1, CENTB1, KIAA0050 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5h3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h3d OCA], [https://pdbe.org/5h3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h3d RCSB], [https://www.ebi.ac.uk/pdbsum/5h3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h3d ProSAT]</span></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=5h3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h3d OCA], [http://pdbe.org/5h3d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h3d RCSB], [http://www.ebi.ac.uk/pdbsum/5h3d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h3d ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACAP1_HUMAN ACAP1_HUMAN]] GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6) required for clathrin-dependent export of proteins from recycling endosomes to trans-Golgi network and cell surface. Required for regulated export of ITGB1 from recycling endosomes to the cell surface and ITGB1-dependent cell migration.<ref>PMID:11062263</ref> <ref>PMID:16256741</ref> <ref>PMID:17398097</ref> <ref>PMID:17664335</ref> <ref>PMID:22645133</ref> | + | [https://www.uniprot.org/uniprot/ACAP1_HUMAN ACAP1_HUMAN] GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6) required for clathrin-dependent export of proteins from recycling endosomes to trans-Golgi network and cell surface. Required for regulated export of ITGB1 from recycling endosomes to the cell surface and ITGB1-dependent cell migration.<ref>PMID:11062263</ref> <ref>PMID:16256741</ref> <ref>PMID:17398097</ref> <ref>PMID:17664335</ref> <ref>PMID:22645133</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Studies on the Bin-Amphiphysin-Rvs (BAR) domain have advanced a fundamental understanding of how proteins deform membrane. We previously showed that a BAR domain in tandem with a Pleckstrin Homology (PH domain) underlies the assembly of ACAP1 (Arfgap with Coil-coil, Ankryin repeat, and PH domain I) into an unusual lattice structure that also uncovers a new paradigm for how a BAR protein deforms membrane. Here, we initially pursued computation-based refinement of the ACAP1 lattice to identify its critical protein contacts. Simulation studies then revealed how ACAP1, which dimerizes into a symmetrical structure in solution, is recruited asymmetrically to the membrane through dynamic behavior. We also pursued electron microscopy (EM)-based structural studies, which shed further insight into the dynamic nature of the ACAP1 lattice assembly. As ACAP1 is an unconventional BAR protein, our findings broaden the understanding of the mechanistic spectrum by which proteins assemble into higher-ordered structures to achieve membrane deformation.
| + | |
| - | | + | |
| - | ACAP1 assembles into an unusual protein lattice for membrane deformation through multiple stages.,Chan C, Pang X, Zhang Y, Niu T, Yang S, Zhao D, Li J, Lu L, Hsu VW, Zhou J, Sun F, Fan J PLoS Comput Biol. 2019 Jul 10;15(7):e1007081. doi: 10.1371/journal.pcbi.1007081. , eCollection 2019 Jul. PMID:31291238<ref>PMID:31291238</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5h3d" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chan, C]] | + | [[Category: Chan C]] |
| - | [[Category: Fan, J]] | + | [[Category: Fan J]] |
| - | [[Category: Pang, X Y]] | + | [[Category: Pang XY]] |
| - | [[Category: Sun, F]] | + | [[Category: Sun F]] |
| - | [[Category: Zhang, Y]] | + | [[Category: Zhang Y]] |
| - | [[Category: Acap1 barph domain]]
| + | |
| - | [[Category: Membrane remodeling]]
| + | |
| - | [[Category: Molecular dynamics simulation]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
ACAP1_HUMAN GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6) required for clathrin-dependent export of proteins from recycling endosomes to trans-Golgi network and cell surface. Required for regulated export of ITGB1 from recycling endosomes to the cell surface and ITGB1-dependent cell migration.[1] [2] [3] [4] [5]
References
- ↑ Jackson TR, Brown FD, Nie Z, Miura K, Foroni L, Sun J, Hsu VW, Donaldson JG, Randazzo PA. ACAPs are arf6 GTPase-activating proteins that function in the cell periphery. J Cell Biol. 2000 Oct 30;151(3):627-38. PMID:11062263
- ↑ Li J, Ballif BA, Powelka AM, Dai J, Gygi SP, Hsu VW. Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent recycling of integrin beta1 to control cell migration. Dev Cell. 2005 Nov;9(5):663-73. PMID:16256741 doi:http://dx.doi.org/S1534-5807(05)00374-6
- ↑ Ma Z, Nie Z, Luo R, Casanova JE, Ravichandran KS. Regulation of Arf6 and ACAP1 signaling by the PTB-domain-containing adaptor protein GULP. Curr Biol. 2007 Apr 17;17(8):722-7. Epub 2007 Mar 29. PMID:17398097 doi:http://dx.doi.org/S0960-9822(07)01115-3
- ↑ Li J, Peters PJ, Bai M, Dai J, Bos E, Kirchhausen T, Kandror KV, Hsu VW. An ACAP1-containing clathrin coat complex for endocytic recycling. J Cell Biol. 2007 Jul 30;178(3):453-64. PMID:17664335 doi:http://dx.doi.org/jcb.200608033
- ↑ Bai M, Pang X, Lou J, Zhou Q, Zhang K, Ma J, Li J, Sun F, Hsu V. Mechanistic insights into regulated cargo binding by ACAP1. J Biol Chem. 2012 May 29. PMID:22645133 doi:10.1074/jbc.M112.378810
|
