View source for 9jih


==Crystal structure of BAR domain of ACAP4==
<StructureSection load='9jih' size='340' side='right'caption='[[9jih]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9jih]] is a 2 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=9JIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9JIH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=9jih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9jih OCA], [https://pdbe.org/9jih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9jih RCSB], [https://www.ebi.ac.uk/pdbsum/9jih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9jih ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ASAP3_HUMAN ASAP3_HUMAN] Promotes cell proliferation.<ref>PMID:14654939</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
ADP-ribosylation factor (Arf)-specific GTPase-activating proteins (ArfGAPs) regulate cell migration through interactions with small G proteins, including Arfs. In ArfGAPs, the Bin/Amphiphysin/Rvs (BAR) domain plays a key role in membrane binding and curvature induction, yet the molecular mechanisms underlying these processes remain unclear. Here, we investigate the function of the BAR domain and its adjacent pleckstrin homology (PH) domain of ACAP4 in cell migration. We demonstrate that the BAR-PH tandem of ACAP4 induces membrane curvature, promotes cell migration, forms condensates in vitro, and exhibits membrane-associated distribution in cells. The crystal structure of the ACAP4 BAR domain, determined at 2.8 A resolution, reveals multiple positively charged surface patches. Structural modeling further identifies conserved positively charged residue pairs in the PH domain, which collectively mediate electrostatic interactions essential for both membrane remodeling and membrane localization. Mutagenesis experiments confirm that these regions are required for ACAP4's subcellular localization and pro-migratory activity. Furthermore, we identify that the actin-binding protein Ezrin interacts with a specific C-terminal region of ACAP4 to regulate its function. Ezrin binding enhances condensate formation and enables full-length ACAP4 to associate with membranes and promote cell migration, particularly when co-expressed with the activated Ezrin (T567D). Together, our findings uncover the molecular basis by which ACAP4 coordinates membrane remodeling and cytoskeletal dynamics, offering new insights into the mechanisms that drive cell migration.

BAR-PH tandem of ACAP4 remodels membranes to drive migration via Ezrin-dependent activation.,Huang S, Chen J, Wang X, Song X, Zhu X, Fu C, Zhang X, Liu X, Wang C J Mol Cell Biol. 2025 Nov 4:mjaf038. doi: 10.1093/jmcb/mjaf038. PMID:41190559<ref>PMID:41190559</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9jih" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chen JS]]
[[Category: Huang S]]
[[Category: Wang C]]