2YMB

Structures of MITD1

Summary for 2YMB

• Entry DOI: 10.2210/pdb2ymb/pdb
• Related: 4A5X 4A5Z
• Descriptor: MIT DOMAIN-CONTAINING PROTEIN 1, CHARGED MULTIVESICULAR BODY PROTEIN 1A (2 entities in total)
• Functional Keywords: protein transport, membrane, pld
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Late endosome membrane; Peripheral membrane protein; Cytoplasmic side: Q8WV92; Cytoplasm: Q9HD42
• Total number of polymer chains: 6
• Total formula weight: 124926.43

Authors

Hadders, M.A.,Agromayor, M.,Obita, T.,Perisic, O.,Caballe, A.,Kloc, M.,Lamers, M.H.,Williams, R.L.,Martin-Serrano, J. (deposition date: 2012-10-08, release date: 2012-10-24, Last modification date: 2023-12-20)

Primary citation

Hadders, M.A.,Agromayor, M.,Obita, T.,Perisic, O.,Caballe, A.,Kloc, M.,Lamers, M.H.,Williams, R.L.,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.USA, 109:17424-, 2012

PubMed Abstract: 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.

PubMed: 23045692
DOI: 10.1073/PNAS.1206839109

Experimental method

X-RAY DIFFRACTION (3.404 Å)