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journal.pgen.1009757 (1).pdf (4.71 MB)

AKTIP interacts with ESCRT I and is needed for the recruitment of ESCRT III subunits to the midbody.

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journal contribution
posted on 2021-09-15, 11:37 authored by Chiara Merigliano, Romina Burla, Mattia La Torre, Simona Del Giudice, Hsiangling Teo, Chong Wai Liew, Alexandre Chojnowski, Wah Ing Goh, Yolanda Olmos, Klizia Maccaroni, Maria Giubettini, Irene Chiolo, Jeremy G Carlton, Domenico Raimondo, Fiammetta Vernì, Colin L Stewart, Daniela Rhodes, Graham D Wright, Brian E Burke, Isabella Saggio
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.


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