Evidence map›Paper›PMID 26153462›Full record

ArticleCellular and molecular life sciences : CMLS2016

A novel family of katanin-like 2 protein isoforms (KATNAL2), interacting with nucleotide-binding proteins Nubp1 and Nubp2, are key regulators of different MT-based processes in mammalian cells.

Antonis Ververis, Andri Christodoulou, Maria Christoforou, Christina Kamilari, Carsten W Lederer, Niovi Santama

Open access · greenAbstract read
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Article in Cellular and molecular life sciences : CMLS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.7field-weighted citation impact, top 18% of its field
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

27 citing papers in PubMed, 40 citations in OpenAlex.

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  9. Knockout ofInternational journal of molecular sciences · 2022
    Article
  10. Article
  11. Article
  12. The Mammalian Family of Katanin Microtubule-Severing Enzymes.Frontiers in cell and developmental biology · 2021
    Review
  13. Article
  14. Review
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  20. Primary cilia proteins: ciliary and extraciliary sites and functions.Cellular and molecular life sciences : CMLS · 2018
    Review
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

6 authors at 2 institutions in 1 country.

Antonis VerverisDepartment of Biological Sciences, University of Cyprus, University Avenue 1, 1678, Nicosia, Cyprus.
Andri ChristodoulouDepartment of Biological Sciences, University of Cyprus, University Avenue 1, 1678, Nicosia, Cyprus.
Maria ChristoforouDepartment of Biological Sciences, University of Cyprus, University Avenue 1, 1678, Nicosia, Cyprus.
Christina KamilariDepartment of Biological Sciences, University of Cyprus, University Avenue 1, 1678, Nicosia, Cyprus.
Carsten W LedererThe Cyprus Institute of Neurology and Genetics, Nicosia, Cyprus.
Niovi SantamaDepartment of Biological Sciences, University of Cyprus, University Avenue 1, 1678, Nicosia, Cyprus. santama@ucy.ac.cy.
University of Cyprus · CYCyprus Institute of Neurology and Genetics · CY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Katanins are microtubule (MT)-severing AAA proteins with high phylogenetic conservation throughout the eukaryotes. They have been functionally implicated in processes requiring MT remodeling, such as spindle assembly in mitosis and meiosis, assembly/disassembly of flagella and cilia and neuronal morphogenesis. Here, we uncover a novel family of katanin-like 2 proteins (KATNAL2) in mouse, consisting of five alternatively spliced isoforms encoded by the Katnal2 genomic locus. We further demonstrate that in vivo these isoforms are able to interact with themselves, with each other and moreover directly and independently with MRP/MinD-type P-loop NTPases Nubp1 and Nubp2, which are integral components of centrioles, negative regulators of ciliogenesis and implicated in centriole duplication in mammalian cells. We find KATNAL2 localized on interphase MTs, centrioles, mitotic spindle, midbody and the axoneme and basal body of sensory cilia in cultured murine cells. shRNAi of Katnal2 results in inefficient cytokinesis and severe phenotypes of enlarged cells and nuclei, increased numbers of centrioles and the manifestation of aberrant multipolar mitotic spindles, mitotic defects, chromosome bridges, multinuclearity, increased MT acetylation and an altered cell cycle pattern. Silencing or stable overexpression of KATNAL2 isoforms drastically reduces ciliogenesis. In conclusion, KATNAL2s are multitasking enzymes involved in the same cell type in critically important processes affecting cytokinesis, MT dynamics, and ciliogenesis and are also implicated in cell cycle progression.

Indexed as

Protein Interaction MapsAdenosine TriphosphatasesAnimalsCell CycleCentrosomeCiliaCytokinesisGene SilencingGTP-Binding ProteinsInterphaseIntracellular Signaling Peptides and ProteinsKataninMiceMicrotubulesNIH 3T3 CellsProtein IsoformsAdenosine TriphosphatasesGTP-Binding ProteinsIntracellular Signaling Peptides and ProteinsKataninKATNAL2 protein, mouseNubp1 protein, mouseNUBP2 protein, mouseProtein IsoformsCiliaCytokinesisCytoskeletonKataninMicrotubule-severing enzymes

Identifiers

PMID26153462
PMCPMC11108477
OpenAlexW848798684

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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.