Evidence map›Paper›PMID 24240191›Full record

ArticleCell cycle (Georgetown, Tex.)2014

Different functions of HOPS isoforms in the cell: HOPS shuttling isoform is determined by RIP cleavage system.

Marilena Castelli, Danilo Piobbico, Daniela Bartoli, Stefania Pieroni, Cinzia Brunacci, Marina Maria Bellet, Martina Chiacchiaretta, Maria Agnese Della Fazia, Giuseppe Servillo

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. International journal of molecular sciences · 2021
    Article
  6. Article
  7. HOPS and p53: thick as thieves in life and death.Cell cycle (Georgetown, Tex.) · 2020
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Liver proliferation: the GUCD1/NEDD4-1 connection.Cell cycle (Georgetown, Tex.) · 2014
    Article
  15. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

Marilena CastelliDepartment of Clinical and Experimental Medicine; University of Perugia; Perugia, Italy.
Danilo PiobbicoDepartment of Clinical and Experimental Medicine; University of Perugia; Perugia, Italy.
Daniela BartoliDepartment of Clinical and Experimental Medicine; University of Perugia; Perugia, Italy.
Stefania PieroniDepartment of Clinical and Experimental Medicine; University of Perugia; Perugia, Italy.
Cinzia BrunacciDepartment of Clinical and Experimental Medicine; University of Perugia; Perugia, Italy.
Marina Maria BelletDepartment of Clinical and Experimental Medicine; University of Perugia; Perugia, Italy.
Martina ChiacchiarettaDepartment of Clinical and Experimental Medicine; University of Perugia; Perugia, Italy.
Maria Agnese Della FaziaDepartment of Clinical and Experimental Medicine; University of Perugia; Perugia, Italy.
Giuseppe ServilloDepartment of Clinical and Experimental Medicine; University of Perugia; Perugia, Italy.
University of Perugia · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hepatocyte odd protein shuttling (HOPS) moves between nucleus and cytoplasm. HOPS overexpression leads to cell cycle arrest in G 0/G 1, and HOPS knockdown causes centrosome alterations, with subsequent abnormal cell division. Recently, we demonstrated that HOPS acts as a functional bridge in NPM-p19(Arf) interactions. Here we show that HOPS is present in 3 different isoforms that play distinct intracellular functions. Although HOPS is a transmembrane ubiquitin, an isoform with intermediate molecular weight is cleaved from the membrane and released into the cytosol, to act as the shuttling protein. We identified a signal peptide peptidase structure in N-terminal membrane-bound HOPS that allows the regulated intramembrane proteolysis (RIP) system to control the relative amounts of the released, shuttling isoform capable of binding NPM. These results argue for distinct, isoform-specific functions of HOPS in the nucleolus, nucleus, and cytoplasm and provide insight into the dynamics of HOPS association with NPM, whose mutation and subsequent delocalization is found in 30% of acute myeloid leukemia patients.

Indexed as

AnimalsCarrier ProteinsCell LineCell NucleusChlorocebus aethiopsComputer SimulationCytosolHumansIntracellular Signaling Peptides and ProteinsMembrane ProteinsMiceNuclear ProteinsNucleophosminOrgan SpecificityProtein BindingProtein ConformationCarrier ProteinsHOPS protein, mouseIntracellular Signaling Peptides and ProteinsMembrane ProteinsNPM1 protein, humanNuclear ProteinsNucleophosminProtein IsoformsTmub1 protein, ratUbiquitinhepatocyte odd protein shuttlingintramembrane-cleaving proteases (iCliPs)/shuttling proteinnucleophosmintransmembrane and ubiquitin-like domain containing 1tumor suppressor gene/regulated intramembrane proteolysis (RIP) system

Identifiers

PMID24240191
PMCPMC3906245
OpenAlexW2030320479

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.