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| | ==The KLC2 TPR domain bound to the JIP3 leucine zipper domain== | | ==The KLC2 TPR domain bound to the JIP3 leucine zipper domain== |
| - | <StructureSection load='6ejn' size='340' side='right' caption='[[6ejn]], [[Resolution|resolution]] 3.20Å' scene=''> | + | <StructureSection load='6ejn' size='340' side='right'caption='[[6ejn]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ejn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EJN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EJN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ejn]] 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=6EJN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EJN FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Klc2, mCG_8395 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Mapk8ip3, Jip3, Jsap1, Syd2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ejn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ejn OCA], [http://pdbe.org/6ejn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ejn RCSB], [http://www.ebi.ac.uk/pdbsum/6ejn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ejn 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=6ejn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ejn OCA], [https://pdbe.org/6ejn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ejn RCSB], [https://www.ebi.ac.uk/pdbsum/6ejn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ejn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/JIP3_MOUSE JIP3_MOUSE]] The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins.<ref>PMID:10523642</ref> <ref>PMID:10629060</ref> | + | [https://www.uniprot.org/uniprot/KLC2_MOUSE KLC2_MOUSE] Kinesin is a microtubule-associated force-producing protein that plays a role in organelle transport. The light chain functions in coupling of cargo to the heavy chain or in the modulation of its ATPase activity. Through binding with PLEKHM2 and ARL8B, recruits kinesin-1 to lysosomes and hence direct lysosomes movement toward microtubule plus ends.[UniProtKB:Q9H0B6] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6ejn" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6ejn" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Kinesin 3D Structures|Kinesin 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Cockburn, J]] | + | [[Category: Mus musculus]] |
| - | [[Category: Hesketh, S J]] | + | [[Category: Cockburn J]] |
| - | [[Category: Way, M]] | + | [[Category: Hesketh SJ]] |
| - | [[Category: Kinesin jip3 transport cargo molecular motor]] | + | [[Category: Way M]] |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
KLC2_MOUSE Kinesin is a microtubule-associated force-producing protein that plays a role in organelle transport. The light chain functions in coupling of cargo to the heavy chain or in the modulation of its ATPase activity. Through binding with PLEKHM2 and ARL8B, recruits kinesin-1 to lysosomes and hence direct lysosomes movement toward microtubule plus ends.[UniProtKB:Q9H0B6]
Publication Abstract from PubMed
Kinesin-1 transports numerous cellular cargoes along microtubules. The kinesin-1 light chain (KLC) mediates cargo binding and regulates kinesin-1 motility. To investigate the molecular basis for kinesin-1 recruitment and activation by cargoes, we solved the crystal structure of the KLC2 tetratricopeptide repeat (TPR) domain bound to the cargo JIP3. This, combined with biophysical and molecular evolutionary analyses, reveals a kinesin-1 cargo binding site, located on KLC TPR1, which is conserved in homologs from sponges to humans. In the complex, JIP3 crosslinks two KLC2 TPR domains via their TPR1s. We show that TPR1 forms a dimer interface that mimics JIP3 binding in all crystal structures of the unbound KLC TPR domain. We propose that cargo-induced dimerization of the KLC TPR domains via TPR1 is a general mechanism for activating kinesin-1. We relate this to activation by tryptophan-acidic cargoes, explaining how different cargoes activate kinesin-1 through related molecular mechanisms.
Insights into Kinesin-1 Activation from the Crystal Structure of KLC2 Bound to JIP3.,Cockburn JJB, Hesketh SJ, Mulhair P, Thomsen M, O'Connell MJ, Way M Structure. 2018 Aug 23. pii: S0969-2126(18)30257-0. doi:, 10.1016/j.str.2018.07.011. PMID:30197037[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cockburn JJB, Hesketh SJ, Mulhair P, Thomsen M, O'Connell MJ, Way M. Insights into Kinesin-1 Activation from the Crystal Structure of KLC2 Bound to JIP3. Structure. 2018 Aug 23. pii: S0969-2126(18)30257-0. doi:, 10.1016/j.str.2018.07.011. PMID:30197037 doi:http://dx.doi.org/10.1016/j.str.2018.07.011
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