|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6qnn' size='340' side='right'caption='[[6qnn]], [[Resolution|resolution]] 2.03Å' scene=''> | | <StructureSection load='6qnn' size='340' side='right'caption='[[6qnn]], [[Resolution|resolution]] 2.03Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6qnn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QNN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QNN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6qnn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QNN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QNN FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CLTC, CLH17, CLTCL2, KIAA0034 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), GTSE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 2.03Å</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=6qnn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qnn OCA], [http://pdbe.org/6qnn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qnn RCSB], [http://www.ebi.ac.uk/pdbsum/6qnn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qnn 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=6qnn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qnn OCA], [https://pdbe.org/6qnn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qnn RCSB], [https://www.ebi.ac.uk/pdbsum/6qnn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qnn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/CLH1_HUMAN CLH1_HUMAN]] Translocation renal cell carcinoma;Inflammatory myofibroblastic tumor. | + | [https://www.uniprot.org/uniprot/CLH1_HUMAN CLH1_HUMAN] Translocation renal cell carcinoma;Inflammatory myofibroblastic tumor. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CLH1_HUMAN CLH1_HUMAN]] Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network. [[http://www.uniprot.org/uniprot/GTSE1_HUMAN GTSE1_HUMAN]] May be involved in p53-induced cell cycle arrest in G2/M phase by interfering with microtubule rearrangements that are required to enter mitosis. Overexpression delays G2/M phase progression. | + | [https://www.uniprot.org/uniprot/CLH1_HUMAN CLH1_HUMAN] Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 20: |
Line 20: |
| | </div> | | </div> |
| | <div class="pdbe-citations 6qnn" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6qnn" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Clathrin 3D structures|Clathrin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lin, Y]] | + | [[Category: Lin Y]] |
| - | [[Category: Porfetye, A T]] | + | [[Category: Porfetye AT]] |
| - | [[Category: Vetter, I R]] | + | [[Category: Vetter IR]] |
| - | [[Category: Beta-propeller]]
| + | |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Clathrin-box]]
| + | |
| - | [[Category: Lidl-motif]]
| + | |
| Structural highlights
Disease
CLH1_HUMAN Translocation renal cell carcinoma;Inflammatory myofibroblastic tumor.
Function
CLH1_HUMAN Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network.
Publication Abstract from PubMed
Clathrin ensures mitotic spindle stability and efficient chromosome alignment, independently of its vesicle trafficking function. Although clathrin localizes to the mitotic spindle and kinetochore fiber microtubule bundles, the mechanisms by which clathrin stabilizes microtubules are unclear. We show that clathrin adaptor interaction sites on clathrin heavy chain (CHC) are repurposed during mitosis to directly recruit the microtubule-stabilizing protein GTSE1 to the spindle. Structural analyses reveal that these sites interact directly with clathrin-box motifs on GTSE1. Disruption of this interaction releases GTSE1 from spindles, causing defects in chromosome alignment. Surprisingly, this disruption destabilizes astral microtubules, but not kinetochore-microtubule attachments, and chromosome alignment defects are due to a failure of chromosome congression independent of kinetochore-microtubule attachment stability. GTSE1 recruited to the spindle by clathrin stabilizes microtubules by inhibiting the microtubule depolymerase MCAK. This work uncovers a novel role of clathrin adaptor-type interactions to stabilize nonkinetochore fiber microtubules to support chromosome congression, defining for the first time a repurposing of this endocytic interaction mechanism during mitosis.
Clathrin's adaptor interaction sites are repurposed to stabilize microtubules during mitosis.,Rondelet A, Lin YC, Singh D, Porfetye AT, Thakur HC, Hecker A, Brinkert P, Schmidt N, Bendre S, Muller F, Mazul L, Widlund PO, Bange T, Hiller M, Vetter IR, Bird AW J Cell Biol. 2020 Feb 3;219(2). pii: 133599. doi: 10.1083/jcb.201907083. PMID:31932847[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rondelet A, Lin YC, Singh D, Porfetye AT, Thakur HC, Hecker A, Brinkert P, Schmidt N, Bendre S, Muller F, Mazul L, Widlund PO, Bange T, Hiller M, Vetter IR, Bird AW. Clathrin's adaptor interaction sites are repurposed to stabilize microtubules during mitosis. J Cell Biol. 2020 Feb 3;219(2). pii: 133599. doi: 10.1083/jcb.201907083. PMID:31932847 doi:http://dx.doi.org/10.1083/jcb.201907083
|
