4a5z: Difference between revisions

Revision as of 07:47, 18 August 2022

Structures of MITD1

Structural highlights

4a5z is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	CL, DMS
NonStd Res:	MSE
Related:	4a5x
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MITD1_HUMAN] Required for efficient abscission at the end of cytokinesis, together with components of the ESCRT-III complex.^[1] ^[2]

Publication Abstract from PubMed

The endosomal sorting complexes required for transport (ESCRT) proteins have a critical function in abscission, the final separation of the daughter cells during cytokinesis. Here, we describe the structure and function of a previously uncharacterized ESCRT-III interacting protein, MIT-domain containing protein 1 (MITD1). Crystal structures of MITD1 reveal a dimer, with a microtubule-interacting and trafficking (MIT) domain at the N terminus and a unique, unanticipated phospholipase D-like (PLD) domain at the C terminus that binds membranes. We show that the MIT domain binds to a subset of ESCRT-III subunits and that this interaction mediates MITD1 recruitment to the midbody during cytokinesis. Depletion of MITD1 causes a distinct cytokinetic phenotype consistent with destabilization of the midbody and abscission failure. These results suggest a model whereby MITD1 coordinates the activity of ESCRT-III during abscission with earlier events in the final stages of cell division.

ESCRT-III binding protein MITD1 is involved in cytokinesis and has an unanticipated PLD fold that binds membranes.,Hadders MA, Agromayor M, Obita T, Perisic O, Caballe A, Kloc M, Lamers MH, Williams RL, Martin-Serrano J Proc Natl Acad Sci U S A. 2012 Oct 8. PMID:23045692^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lee S, Chang J, Renvoise B, Tipirneni A, Yang S, Blackstone C. MITD1 is recruited to midbodies by ESCRT-III and participates in cytokinesis. Mol Biol Cell. 2012 Nov;23(22):4347-61. doi: 10.1091/mbc.E12-04-0292. Epub 2012, Sep 26. PMID:23015756 doi:https://dx.doi.org/10.1091/mbc.E12-04-0292
↑ Hadders MA, Agromayor M, Obita T, Perisic O, Caballe A, Kloc M, Lamers MH, Williams RL, Martin-Serrano J. ESCRT-III binding protein MITD1 is involved in cytokinesis and has an unanticipated PLD fold that binds membranes. Proc Natl Acad Sci U S A. 2012 Oct 8. PMID:23045692 doi:https://dx.doi.org/10.1073/pnas.1206839109
↑ Hadders MA, Agromayor M, Obita T, Perisic O, Caballe A, Kloc M, Lamers MH, Williams RL, Martin-Serrano J. ESCRT-III binding protein MITD1 is involved in cytokinesis and has an unanticipated PLD fold that binds membranes. Proc Natl Acad Sci U S A. 2012 Oct 8. PMID:23045692 doi:https://dx.doi.org/10.1073/pnas.1206839109

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Lee S, Chang J, Renvoise B, Tipirneni A, Yang S, Blackstone C. MITD1 is recruited to midbodies by ESCRT-III and participates in cytokinesis. Mol Biol Cell. 2012 Nov;23(22):4347-61. doi: 10.1091/mbc.E12-04-0292. Epub 2012, Sep 26. PMID:23015756 doi:https://dx.doi.org/10.1091/mbc.E12-04-0292

[2] Hadders MA, Agromayor M, Obita T, Perisic O, Caballe A, Kloc M, Lamers MH, Williams RL, Martin-Serrano J. ESCRT-III binding protein MITD1 is involved in cytokinesis and has an unanticipated PLD fold that binds membranes. Proc Natl Acad Sci U S A. 2012 Oct 8. PMID:23045692 doi:https://dx.doi.org/10.1073/pnas.1206839109

[3] Hadders MA, Agromayor M, Obita T, Perisic O, Caballe A, Kloc M, Lamers MH, Williams RL, Martin-Serrano J. ESCRT-III binding protein MITD1 is involved in cytokinesis and has an unanticipated PLD fold that binds membranes. Proc Natl Acad Sci U S A. 2012 Oct 8. PMID:23045692 doi:https://dx.doi.org/10.1073/pnas.1206839109

[1]

[2]

[3]

@@ Line 3: / Line 3: @@
 <StructureSection load='4a5z' size='340' side='right'caption='[[4a5z]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4a5z]] is a 4 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=4A5Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A5Z FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4a5z]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A5Z FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a5x|4a5x]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4a5x|4a5x]]</div></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=4a5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a5z OCA], [http://pdbe.org/4a5z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a5z RCSB], [http://www.ebi.ac.uk/pdbsum/4a5z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a5z 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=4a5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a5z OCA], [https://pdbe.org/4a5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a5z RCSB], [https://www.ebi.ac.uk/pdbsum/4a5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a5z ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MITD1_HUMAN MITD1_HUMAN]] Required for efficient abscission at the end of cytokinesis, together with components of the ESCRT-III complex.<ref>PMID:23015756</ref> <ref>PMID:23045692</ref>
+[[https://www.uniprot.org/uniprot/MITD1_HUMAN MITD1_HUMAN]] Required for efficient abscission at the end of cytokinesis, together with components of the ESCRT-III complex.<ref>PMID:23015756</ref> <ref>PMID:23045692</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 25: / Line 25: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Agromayor, M]]
 [[Category: Caballe, A]]

4a5z: Difference between revisions

Revision as of 07:47, 18 August 2022

Structures of MITD1

Structural highlights

Function

Publication Abstract from PubMed

References

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