Evidence map›Paper›PMID 40596417›Full record

ArticleScientific reports2025

The localisation and stability of the CENP-F protein are regulated by importin beta and microtubules in mitotic cells.

Ludovica Altieri, Michela Damizia, Paola Rovella, Vincenzo Costanzo, Morena Mancini, Patrizio Di Micco, Matteo Marzi, Daniela Trisciuoglio, Veronica Morea, Patrizia Lavia

Abstract read
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Review
  2. Non-transport functions of motor proteins in corticogenesis.Frontiers in cell and developmental biology · 2026
    Review
  3. Article
  4. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Ludovica AltieriInstitute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, 00185, Rome, Italy.
Michela DamiziaInstitute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, 00185, Rome, Italy.
Paola RovellaInstitute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, 00185, Rome, Italy.
Vincenzo CostanzoInstitute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, 00185, Rome, Italy.
Morena ManciniDepartment of Biology and Biotechnology "Charles Darwin", Sapienza University of Rome, 00185, Rome, Italy.
Patrizio Di MiccoInstitute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, 00185, Rome, Italy.
Matteo MarziDepartment of Biology and Biotechnology "Charles Darwin", Sapienza University of Rome, 00185, Rome, Italy.
Daniela TrisciuoglioInstitute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, 00185, Rome, Italy.
Veronica MoreaInstitute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, 00185, Rome, Italy.
Patrizia LaviaInstitute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, 00185, Rome, Italy. patrizia.lavia@cnr.it.

Funding

Associazione Italiana per la Ricerca sul Cancro IG2020-24942Italian Ministry of University and Research (MUR) PRIN 2017483NH8_005Italian Ministry of University and Research (MUR) PRIN 2017FNZRN3_005
6 · The paper itself

Abstract

CENP-F is a large protein acting in fundamental cell cycle processes, including nuclear envelope breakdown, mitotic microtubule function and chromosome segregation. These activities are mediated by specific CENP-F protein elements that interact with microtubules, motor proteins, centrosomes and kinetochores. CENP-F is then ubiquitinated and degraded in late mitosis. The C-terminal region of CENP-F contains regulatory elements, including a region required for nuclear localisation in interphase and a KEN box driving proteolysis in late mitosis. Here we show that CENP-F generates proximity ligation products with importin beta during mitosis. Furthermore, induction of importin beta overexpression influences CENP-F at two levels: it alters CENP-F mitotic localisation, promoting its accumulation at spindle poles and decreasing its association with kinetochores, and also causes its persistence in the late mitotic window in which CENP-F normally disappears, in a process that requires microtubule integrity and dynamics. These data implicate therefore importin beta in spatial and temporal control of CENP-F during mitosis, and uncover a functional interplay between CENP-F's ability to regulate mitotic microtubules and, in turn, a protective role of microtubules against CENP-F premature ubiquitination.

Indexed as

beta KaryopherinsChromosomal Proteins, Non-HistoneMicrotubulesMitosisHeLa CellsHumansKinetochoresMicrofilament ProteinsProtein StabilitySpindle ApparatusUbiquitinationbeta Karyopherinscentromere protein FChromosomal Proteins, Non-HistoneMicrofilament ProteinsCENP-FImportin betaKinetochoresMicrotubulesMitotic spindle polesProtein stability

Identifiers

PMID40596417
PMCPMC12216719

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.