View source for 6jmu


==Crystal structure of GIT1/Paxillin complex==
<StructureSection load='6jmu' size='340' side='right'caption='[[6jmu]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6jmu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JMU 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&#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=6jmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jmu OCA], [https://pdbe.org/6jmu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jmu RCSB], [https://www.ebi.ac.uk/pdbsum/6jmu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jmu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GIT1_MOUSE GIT1_MOUSE] GTPase-activating protein for the ADP ribosylation factor family. May serve as a scaffold to bring together molecules to form signaling modules controlling vesicle trafficking, adhesion and cytoskeletal organization. Increases the speed of cell migration, as well as the size and rate of formation of protrusions, possibly by targeting PAK1 to adhesions and the leading edge of lamellipodia. Sequesters inactive non-tyrosine-phosphorylated paxillin in cytoplasmic complexes (By similarity). Involved in the regulation of cytokinesis; the function may involve ENTR1 and PTPN13 (PubMed:23108400).<ref>PMID:23108400</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enzymes or enzyme complexes can be concentrated in different cellular loci to modulate distinct functional processes in response to specific signals. How cells condense and compartmentalize enzyme complexes for spatiotemporally distinct cellular events is not well understood. Here we discover that specific and tight association of GIT1 and beta-Pix, a pair of GTPase regulatory enzymes, leads to phase separation of the complex without additional scaffolding molecules. GIT1/beta-Pix condensates are modular in nature and can be positioned at distinct cellular compartments, such as neuronal synapses, focal adhesions, and cell-cell junctions, by upstream adaptors. Guided by the structure of the GIT/PIX complex, we specifically probed the role of phase separation of the enzyme complex in cell migration and synapse formation. Our study suggests that formation of modular enzyme complex condensates via phase separation can dynamically concentrate limited quantities of enzymes to distinct cellular compartments for specific and optimal signaling.

GIT/PIX Condensates Are Modular and Ideal for Distinct Compartmentalized Cell Signaling.,Zhu J, Zhou Q, Xia Y, Lin L, Li J, Peng M, Zhang R, Zhang M Mol Cell. 2020 Sep 3;79(5):782-796.e6. doi: 10.1016/j.molcel.2020.07.004. Epub, 2020 Aug 10. PMID:32780989<ref>PMID:32780989</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jmu" style="background-color:#fffaf0;"></div>

==See Also==
*[[Paxillin|Paxillin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Lin L]]
[[Category: Xia Y]]
[[Category: Zhang M]]
[[Category: Zhang R]]
[[Category: Zhu J]]