8iw5
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8iw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8iw5 OCA], [https://pdbe.org/8iw5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8iw5 RCSB], [https://www.ebi.ac.uk/pdbsum/8iw5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8iw5 ProSAT]</span></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=8iw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8iw5 OCA], [https://pdbe.org/8iw5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8iw5 RCSB], [https://www.ebi.ac.uk/pdbsum/8iw5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8iw5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Function == | ||
| - | [https://www.uniprot.org/uniprot/LIPB1_MOUSE LIPB1_MOUSE] May regulate the disassembly of focal adhesions. Did not bind receptor-like tyrosine phosphatases type 2A (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Focal adhesions (FAs) are dynamic protein assemblies that connect cytoskeletons to the extracellular matrix and are crucial for cell adhesion and migration. KANKs are scaffold proteins that encircle FAs and act as key regulators of FA dynamics, but the molecular mechanism underlying their specified localization and functions remains poorly understood. Here, we determine the KANK1 structures in complex with talin and liprin-beta, respectively. These structures, combined with our biochemical and cellular analyses, demonstrate how KANK1 scaffolds the FA core and associated proteins to modulate the FA shape in response to mechanical force. Additionally, we find that KANK1 undergoes liquid-liquid phase separation (LLPS), which is important for its localization at the FA edge and cytoskeleton connections to FAs. Our findings not only indicate the molecular basis of KANKs in bridging the core and periphery of FAs but also provide insights into the LLPS-mediated dynamic regulation of FA morphology. | Focal adhesions (FAs) are dynamic protein assemblies that connect cytoskeletons to the extracellular matrix and are crucial for cell adhesion and migration. KANKs are scaffold proteins that encircle FAs and act as key regulators of FA dynamics, but the molecular mechanism underlying their specified localization and functions remains poorly understood. Here, we determine the KANK1 structures in complex with talin and liprin-beta, respectively. These structures, combined with our biochemical and cellular analyses, demonstrate how KANK1 scaffolds the FA core and associated proteins to modulate the FA shape in response to mechanical force. Additionally, we find that KANK1 undergoes liquid-liquid phase separation (LLPS), which is important for its localization at the FA edge and cytoskeleton connections to FAs. Our findings not only indicate the molecular basis of KANKs in bridging the core and periphery of FAs but also provide insights into the LLPS-mediated dynamic regulation of FA morphology. | ||
| - | KANK1 shapes focal adhesions by orchestrating protein binding, mechanical force sensing, and phase separation.,Guo K, Zhang J, Huang P, Xu Y, Pan W, Li K, Chen L, Luo L, Yu W, Chen S, He S, Wei Z, Yu C Cell Rep. 2023 | + | KANK1 shapes focal adhesions by orchestrating protein binding, mechanical force sensing, and phase separation.,Guo K, Zhang J, Huang P, Xu Y, Pan W, Li K, Chen L, Luo L, Yu W, Chen S, He S, Wei Z, Yu C Cell Rep. 2023 Nov 28;42(11):113321. doi: 10.1016/j.celrep.2023.113321. Epub 2023 , Oct 23. PMID:37874676<ref>PMID:37874676</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
Crystal structure of liprin-beta H2H3 dimer
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Categories: Large Structures | Mus musculus | Chen S | Wei Z | Zhang J
