1y19
From Proteopedia
(Difference between revisions)
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<StructureSection load='1y19' size='340' side='right'caption='[[1y19]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='1y19' size='340' side='right'caption='[[1y19]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1y19]] is a 12 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1y19]] is a 12 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=1Y19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y19 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</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=1y19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y19 OCA], [https://pdbe.org/1y19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y19 RCSB], [https://www.ebi.ac.uk/pdbsum/1y19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y19 ProSAT]</span></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/PI51C_MOUSE PI51C_MOUSE] Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). PtdIns(4,5)P2 is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. The majority of PtdIns(4,5)P2 is thought to occur via type I phosphatidylinositol 4-phosphate 5-kinases given the abundance of PtdIns4P. Participates in a variety of cellular processes such as vesicle mediated transport, cell adhesion, cell polarization and cell migration. Together with PIP5K1A is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle attachment by generating the pool of PtdIns(4,5)P2 that induces controlled actin depolymerization to facilitate Fc-gamma-R clustering. Mediates RAC1-dependent reorganization of actin filaments. Required for synaptic vesicle transport. Controls the plasma membrane pool of PtdIns(4,5)P2 implicated in synaptic vesicle endocytosis and exocytosis. Plays a role in endocytosis mediated by clathrin and AP-2 (adaptor protein complex 2). Required for clathrin-coated pits assembly at the synapse. Participates in cell junction assembly. Modulates adherens junctions formation by facilitating CDH1 trafficking. Required for focal adhesion dynamics. Modulates the targeting of talins (TLN1 and TLN2) to the plasma membrane and their efficient assembly into focal adhesions. Regulates the interaction between talins (TLN1 and TLN2) and beta-integrins. Required for uropodium formation and retraction of the cell rear during directed migration. Has a role in growth factor- stimulated directional cell migration and adhesion. Required for talin assembly into nascent adhesions forming at the leading edge toward the direction of the growth factor. Negative regulator of T-cell activation and adhesion. Negatively regulates integrin alpha-L/beta-2 (LFA-1) polarization and adhesion induced by T-cell receptor. Together with PIP5K1A have a role during embryogenesis and together with PIP5K1B may have a role immediately after birth.<ref>PMID:9535851</ref> <ref>PMID:12422220</ref> <ref>PMID:15386003</ref> <ref>PMID:16707488</ref> <ref>PMID:17635937</ref> <ref>PMID:17928408</ref> <ref>PMID:17609388</ref> <ref>PMID:19153220</ref> <ref>PMID:20622009</ref> <ref>PMID:20855869</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
- | *[[Talin|Talin]] | + | *[[Talin 3D structures|Talin 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Mus musculus]] |
- | [[Category: Bate | + | [[Category: Bate N]] |
- | [[Category: Campbell | + | [[Category: Campbell ID]] |
- | [[Category: Critchley | + | [[Category: Critchley DR]] |
- | [[Category: Ginsberg | + | [[Category: Ginsberg MH]] |
- | [[Category: Liddington | + | [[Category: Liddington RC]] |
- | + | [[Category: Santelli E]] | |
- | [[Category: Santelli | + | [[Category: Wegener K]] |
- | [[Category: Wegener | + | [[Category: De Pereda JM]] |
- | [[Category: | + | |
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Revision as of 07:59, 15 May 2024
Structural basis for phosphatidylinositol phosphate kinase type I-gamma binding to talin at focal adhesions
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