Evidence map›Paper›PMID 31462741›Full record

ArticleScientific reports2019

Proximity interactions of the ubiquitin ligase Mind bomb 1 reveal a role in regulation of epithelial polarity complex proteins.

Sascha E Dho, Nancy Silva-Gagliardi, Fabio Morgese, Etienne Coyaud, Emily Lamoureux, Donna M Berry, Brian Raught, C Jane McGlade

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

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  14. E3 ubiquitin ligase Mindbomb 1 facilitates nuclear delivery of adenovirus genomes.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Tools for Decoding Ubiquitin Signaling in DNA Repair.Frontiers in cell and developmental biology · 2021
    Review
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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

8 authors at 3 institutions in 2 countries.

Sascha E DhoProgram in Cell Biology and The Arthur and Sonia Brain Tumour Research Centre, The Hospital for Sick Children, 555 University Ave., Toronto, ON, M5G 1X8, Canada.
Nancy Silva-GagliardiProgram in Cell Biology and The Arthur and Sonia Brain Tumour Research Centre, The Hospital for Sick Children, 555 University Ave., Toronto, ON, M5G 1X8, Canada.
Fabio MorgeseProgram in Cell Biology and The Arthur and Sonia Brain Tumour Research Centre, The Hospital for Sick Children, 555 University Ave., Toronto, ON, M5G 1X8, Canada.
Etienne CoyaudPrincess Margaret Cancer Centre, University Health Network, Toronto, ON, M5G 1L7, Canada.
Emily LamoureuxProgram in Cell Biology and The Arthur and Sonia Brain Tumour Research Centre, The Hospital for Sick Children, 555 University Ave., Toronto, ON, M5G 1X8, Canada.
Donna M BerryProgram in Cell Biology and The Arthur and Sonia Brain Tumour Research Centre, The Hospital for Sick Children, 555 University Ave., Toronto, ON, M5G 1X8, Canada.
Brian RaughtPrincess Margaret Cancer Centre, University Health Network, Toronto, ON, M5G 1L7, Canada.
C Jane McGladeProgram in Cell Biology and The Arthur and Sonia Brain Tumour Research Centre, The Hospital for Sick Children, 555 University Ave., Toronto, ON, M5G 1X8, Canada. jmcglade@sickkids.ca.ORCID http://orcid.org/0000-0001-9605-246X
Hospital for Sick Children · CAUniversity Health Network · CAUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MIB1 belongs to the RING domain containing family of E3 ubiquitin ligases. In vertebrates, MIB1 plays an essential role in activation of Notch signaling during development, through the ubiquitination and endocytosis of Notch ligands. More recently, Notch independent functions for MIB1 have been described in centriole homeostasis, dendritic spine outgrowth and directional cell migration. Here we use proximity-dependent biotin identification (BioID) to define the MIB1 interactome that included 163 high confidence interactions with polypeptides linked to centrosomes and cilia, endosomal trafficking, RNA and DNA processing, the ubiquitin system, and cell adhesion. Biochemical analysis identified several proteins within these groups including CCDC14 and EPS15 that were ubiquitinated but not degraded when co-expressed with MIB1. The MIB1 interactome included the epithelial cell polarity protein, EPB41L5. MIB1 binds to and ubiquitinates EPB41L5 resulting in its degradation. Furthermore, MIB1 ubiquitinates the EPB41L5-associated polarity protein CRB1, an important determinant of the apical membrane. In polarized cells, MIB1 localized to the lateral membrane with EPB41L5 and to the tight junction with CRB1, CRB3 and ZO1. Furthermore, over expression of MIB1 resulted in altered epithelial cell morphology and apical membrane expansion. These results support a role for MIB1 in regulation of polarized epithelial cell morphology.

Indexed as

Cell PolarityUbiquitinationAdaptor Proteins, Signal TransducingEpithelial CellsEye ProteinsHEK293 CellsHeLa CellsHumansMembrane GlycoproteinsMembrane ProteinsNerve Tissue ProteinsTight JunctionsUbiquitin-Protein LigasesZonula Occludens-1 ProteinAdaptor Proteins, Signal TransducingCCDC141 protein, humanCRB1 protein, humanCRB3 protein, humanEPB41L5 protein, humanEPS15 protein, humanEye ProteinsMembrane GlycoproteinsMembrane ProteinsMIB1 ligase, humanNerve Tissue ProteinsTJP1 protein, humanUbiquitin-Protein LigasesZonula Occludens-1 Protein

Identifiers

PMID31462741
PMCPMC6713736
OpenAlexW2971295875

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.