RT Journal Article
T1 AKTIP interacts with ESCRT I and is needed for the recruitment of ESCRT III subunits to the midbody
A1 Merigliano, Chiara
A1 Burla, Romina
A1 La Torre, Mattia
A1 Del Giudice, Simona
A1 Teo, Hsiangling
A1 Liew, Chong Wai
A1 Chojnowski, Alexandre
A1 Goh, Wah Ing Goh
A1 Olmos Buchelt, Yolanda
A1 Maccaroni, Klizia
A1 Giubettini, Maria
A1 Chiolo, Irene
A1 Carlton, Jeremy G.
A1 Raimondo, Domenico
A1 Vernì, Fiammetta
A1 Stewart, Colin L.
A1 Rhodes, Daniela
A1 Wright, Graham D.
A1 Burke, Brian E.
A1 Saggio, Isabella
AB To complete mitosis, the bridge that links the two daughter cells needs to be cleaved. This step is carried out by the endosomal sorting complex required for transport (ESCRT) machinery. AKTIP, a protein discovered to be associated with telomeres and the nuclear membrane in interphase cells, shares sequence similarities with the ESCRT I component TSG101. Here we present evidence that during mitosis AKTIP is part of the ESCRT machinery at the midbody. AKTIP interacts with the ESCRT I subunit VPS28 and forms a circular supra-structure at the midbody, in close proximity with TSG101 and VPS28 and adjacent to the members of the ESCRT III module CHMP2A, CHMP4B and IST1. Mechanistically, the recruitment of AKTIP is dependent on MKLP1 and independent of CEP55. AKTIP and TSG101 are needed together for the recruitment of the ESCRT III subunit CHMP4B and in parallel for the recruitment of IST1. Alone, the reduction of AKTIP impinges on IST1 and causes multinucleation. Our data altogether reveal that AKTIP is a component of the ESCRT I module and functions in the recruitment of ESCRT III components required for abscission.
PB Public Library of Science
SN 1553-7390
YR 2021
FD 2021-08-27
LK https://hdl.handle.net/20.500.14352/105010
UL https://hdl.handle.net/20.500.14352/105010
LA eng
NO Merigliano C, Burla R, La Torre M, Del Giudice S, Teo H, Liew CW, et al. Copenhaver GP, editor. AKTIP interacts with ESCRT I and is needed for the recruitment of ESCRT III subunits to the midbody. PLoS Genet. 2021;17(8):e1009757.
NO Funding: This work was supported by PRF 2016-67, Progetti di Ricerca, Sapienza University of Rome (RP1181642E87148C), AIRC IG-24614 to IS, FIRC (22392) to MLT and IS, CIB (http://www.cibiotech.it/) and Fondazione Buzzati Traverso (813 - https://www.fondazioneadrianobuzzatitraverso.it) to MLT and IS; Avvio alla Ricerca, Sapienza University of Rome (AR2181642B6F2E48, AR1181642EE61111) to RB, SDG and IS. CM has been supported by EMBO ST fellowship 7621, Veronesi TG 2019. MLT is supported by Be For ERC, Sapienza. IC is supported by R01GM117376 and NSF Career 1751197. JGC is supported by a Wellcome Trust Senior Research Fellowship 206346/Z/17/Z. This work was supported in part by the Francis Crick Institute which receives its core funding from Cancer Research UK (FC001002), the UK Medical Research Council (FC001002), and the Wellcome Trust (FC001002). For the purpose of Open Access, the author has applied a CC BY public copyright licence to any Author Accepted Manuscript version arising from this submission. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
DS Docta Complutense
RD 1 ene 2026