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| | ==Localisation of Dynein Light Chains 1 and 2 and their Pro-apoptotic Ligands== | | ==Localisation of Dynein Light Chains 1 and 2 and their Pro-apoptotic Ligands== |
| - | <StructureSection load='1re6' size='340' side='right' caption='[[1re6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1re6' size='340' side='right'caption='[[1re6]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1re6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RE6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RE6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1re6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RE6 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DLC2 ([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">Solution NMR</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=1re6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1re6 OCA], [http://pdbe.org/1re6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1re6 RCSB], [http://www.ebi.ac.uk/pdbsum/1re6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1re6 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=1re6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1re6 OCA], [https://pdbe.org/1re6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1re6 RCSB], [https://www.ebi.ac.uk/pdbsum/1re6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1re6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DYL2_MOUSE DYL2_MOUSE] Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1re6" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1re6" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Dynein 3D structures|Dynein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Barsukov, I]] | + | [[Category: Mus musculus]] |
| - | [[Category: Day, C L]] | + | [[Category: Barsukov I]] |
| - | [[Category: Hinds, M G]] | + | [[Category: Day CL]] |
| - | [[Category: Huang, D C]] | + | [[Category: Hinds MG]] |
| - | [[Category: Lian, L Y]] | + | [[Category: Huang DC]] |
| - | [[Category: Puthalakath, H]] | + | [[Category: Lian LY]] |
| - | [[Category: Skea, G]] | + | [[Category: Puthalakath H]] |
| - | [[Category: Strasser, A]] | + | [[Category: Skea G]] |
| - | [[Category: Apoptosis]]
| + | [[Category: Strasser A]] |
| - | [[Category: Contractile protein]]
| + | |
| - | [[Category: Dimer]]
| + | |
| - | [[Category: Dynein light chain]]
| + | |
| Structural highlights
Function
DYL2_MOUSE Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The dynein and myosin V motor complexes are multi-protein structures that function to transport molecules and organelles within the cell. DLC (dynein light-chain) proteins, found as components of both dynein and myosin V motor complexes, connect the complexes to their cargoes. One of the roles of these motor complexes is to selectively sequester the pro-apoptotic 'BH3-only' (Bcl-2 homology 3-only) proteins, Bim (Bcl-2-interacting mediator of cell death) and Bmf (Bcl-2-modifying factor), and so regulate their cell death-inducing function. In vivo DLC2 is found exclusively as a component of the myosin V motor complex and Bmf binds DLC2 selectively. On the other hand, Bim interacts with DLC1 (LC8), an integral component of the dynein motor complex. The two DLCs share 93% sequence identity yet show unambiguous in vivo specificity for their respective BH3-only ligands. To investigate this specificity the three-dimensional solution structure of DLC2 was elucidated using NMR spectroscopy. In vitro structural and mutagenesis studies show that Bmf and Bim have identical binding characteristics to recombinant DLC2 or DLC1. Thus the selectivity shown by Bmf and Bim for binding DLC1 or DLC2, respectively, does not reside in their DLC-binding domains. Remarkably, mutational analysis of DLC1 and DLC2 indicates that a single surface residue (residue 41) determines the specific localization of DLCs with their respective motor complexes. These results suggest a molecular mechanism for the specific compartmentalization of DLCs and their pro-apoptotic cargoes and implicate other protein(s) in defining the specificity between the cargoes and the DLC proteins.
Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands.,Day CL, Puthalakath H, Skea G, Strasser A, Barsukov I, Lian LY, Huang DC, Hinds MG Biochem J. 2004 Feb 1;377(Pt 3):597-605. PMID:14561217[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Day CL, Puthalakath H, Skea G, Strasser A, Barsukov I, Lian LY, Huang DC, Hinds MG. Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands. Biochem J. 2004 Feb 1;377(Pt 3):597-605. PMID:14561217 doi:10.1042/BJ20031251
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