Document Detail


ESCRT-III binding protein MITD1 is involved in cytokinesis and has an unanticipated PLD fold that binds membranes.
MedLine Citation:
PMID:  23045692     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Michael A Hadders; Monica Agromayor; Takayuki Obita; Olga Perisic; Anna Caballe; Magdalena Kloc; Meindert H Lamers; Roger L Williams; Juan Martin-Serrano
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-10-08
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  109     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-24     Completed Date:  2013-01-07     Revised Date:  2014-02-20    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  17424-9     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Crystallography, X-Ray
Cytokinesis / physiology*
Endosomal Sorting Complexes Required for Transport / metabolism*
HeLa Cells
Humans
Membrane Proteins / chemistry,  metabolism,  physiology*
Microtubule-Associated Proteins / chemistry,  metabolism,  physiology*
Models, Molecular
Phospholipase D / metabolism*
Protein Binding
Protein Folding
Grant Support
ID/Acronym/Agency:
083639/Z/07/Z//Biotechnology and Biological Sciences Research Council; G0802777//Medical Research Council; MC_U105184308//Medical Research Council; MC_U105197143//Medical Research Council; WT093056MA//Wellcome Trust
Chemical
Reg. No./Substance:
0/Endosomal Sorting Complexes Required for Transport; 0/MITD1 protein, human; 0/Membrane Proteins; 0/Microtubule-Associated Proteins; EC 3.1.4.4/Phospholipase D
Comments/Corrections

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