Evidence map›Paper›PMID 30516430›Full record

ArticleMolecular biology of the cell2019

SUMOylation of periplakin is critical for efficient reorganization of keratin filament network.

Mansi Gujrati, Rohit Mittal, Lakhan Ekal, Ram Kumar Mishra

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

8 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Genomic adaptations for arboreal locomotion in Asian flying treefrogs.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Keratins as an Inflammation Trigger Point in Epidermolysis Bullosa Simplex.International journal of molecular sciences · 2021
    Review
  8. 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

4 authors at 3 institutions in 2 countries.

Mansi GujratiNups and SUMO Biology Group, Department of Biological Sciences, Indian Institute of Science Education and Research (IISER) Bhopal, Madhya Pradesh 462066, India.
Rohit MittalMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Lakhan EkalDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, UK.
Ram Kumar MishraNups and SUMO Biology Group, Department of Biological Sciences, Indian Institute of Science Education and Research (IISER) Bhopal, Madhya Pradesh 462066, India.
Indian Institute of Science Education and Research, Bhopal · INMRC Laboratory of Molecular Biology · GBUniversity of Sheffield · GB

Funding

Medical Research Council MC_U105178795
6 · The paper itself

Abstract

The architecture of the cytoskeleton and its remodeling are tightly regulated by dynamic reorganization of keratin-rich intermediate filaments. Plakin family proteins associate with the network of intermediate filaments (IFs) and affect its reorganization during migration, differentiation, and response to stress. The smallest plakin, periplakin (PPL), interacts specifically with intermediate filament proteins K8, K18, and vimentin via its C-terminal linker domain. Here, we show that periplakin is SUMOylated at a conserved lysine in its linker domain (K1646) preferentially by small ubiquitin-like modifier 1 (SUMO1). Our data indicate that PPL SUMOylation is essential for the proper reorganization of the keratin IF network. Stresses perturbing intermediate-filament and cytoskeletal architecture induce hyper--SUMOylation of periplakin. Okadaic acid induced hyperphosphorylation-dependent collapse of the keratin IF network results in a similar hyper-SUMOylation of PPL. Strikingly, exogenous overexpression of a non-SUMOylatable periplakin mutant (K1646R) induced aberrant bundling and loose network interconnections of the keratin filaments. Time-lapse imaging of cells expressing the K1646R mutant showed the enhanced sensitivity of keratin filament collapse upon okadaic acid treatment. Our data identify an important regulatory role for periplakin SUMOylation in dynamic reorganization and stability of keratin IFs.

Indexed as

SumoylationAmino Acid SequenceConserved SequenceCytoskeletonGreen Fluorescent ProteinsHEK293 CellsHeLa CellsHumansIntermediate FilamentsKeratinsLysineModels, BiologicalPlakinsProtein DomainsStress, PhysiologicalGreen Fluorescent ProteinsKeratinsLysinePlakinsPPL protein, human

Identifiers

PMID30516430
PMCPMC6589569
OpenAlexW2902990744

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.