Evidence map›Paper›PMID 19549684›Full record

ArticleJournal of cell science2009

Rescue of atypical protein kinase C in epithelia by the cytoskeleton and Hsp70 family chaperones.

Anastasia Mashukova, Andrea S Oriolo, Flavia A Wald, M Llanos Casanova, Cornelia Kröger, Thomas M Magin, M Bishr Omary, Pedro J I Salas

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
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  5. Modulation of epithelial cell polarity by bacterial pathogens.Annals of the New York Academy of Sciences · 2017
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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 4 institutions in 3 countries.

Anastasia MashukovaDepartment of Cell Biology and Anatomy, University of Miami Miller School of Medicine, Miami, FL 33136, USA.
Andrea S Oriolo
Flavia A Wald
M Llanos Casanova
Cornelia Kröger
Thomas M Magin
M Bishr Omary
Pedro J I Salas
University of Miami · USUniversity of Bonn · DEUnidades Centrales Científico-Técnicas · ESUniversity of Michigan–Ann Arbor · US

Funding

Keratin Biology and Disease Aspects in Simple EpitheliaR01DK047918 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI OMARY, BISHR · 1995 to 2018
$6.6M
Apical Polarity Complex Signaling in Inflammation in Intestinal EpitheliaR01DK076652 · NIDDK · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI SALAS, PEDRO · 2007 to 2015
$2.9M
Apical intermediate filament (IF) mediated post ischemia recovery in epitheliaR01DK057805 · NIDDK · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI SALAS, PEDRO · 2001 to 2009
$2.2M
NIDDK NIH HHS R01 DK047918NIDDK NIH HHS R01 DK057805NIDDK NIH HHS R01DK057805NIDDK NIH HHS R01 DK076652NIDDK NIH HHS R01DK076652NIDDK NIH HHS R01DK47918
6 · The paper itself

Abstract

Atypical PKC (PKC iota) is a key organizer of cellular asymmetry. Sequential extractions of intestinal cells showed a pool of enzymatically active PKC iota and the chaperone Hsp70.1 attached to the apical cytoskeleton. Pull-down experiments using purified and recombinant proteins showed a complex of Hsp70 and atypical PKC on filamentous keratins. Transgenic animals overexpressing keratin 8 displayed delocalization of Hsp70 and atypical PKC. Two different keratin-null mouse models, as well as keratin-8 knockdown cells in tissue culture, also showed redistribution of Hsp70 and a sharp decrease in the active form of atypical PKC, which was also reduced by Hsp70 knockdown. An in-vitro turn motif rephosphorylation assay indicated that PKC iota is dephosphorylated by prolonged activity. The Triton-soluble fraction could rephosphorylate PKC iota only when supplemented with the cytoskeletal pellet or filamentous highly purified keratins, a function abolished by immunodepletion of Hsp70 but rescued by recombinant Hsp70. We conclude that both filamentous keratins and Hsp70 are required for the rescue rephosphorylation of mature atypical PKC, regulating the subcellular distribution and steady-state levels of active PKC iota.

Indexed as

AnimalsCaco-2 CellsEnterocytesHSP70 Heat-Shock ProteinsHumansIntermediate FilamentsIsoenzymesKeratin-18Keratin-19Keratin-8KeratinsMiceMice, Inbred C57BLMice, KnockoutMice, TransgenicPhosphorylationheat-shock protein 70.1HSP70 Heat-Shock ProteinsIsoenzymesKeratin-18Keratin-19Keratin-8KeratinsKrt8 protein, mouseProtein Kinase CProtein Kinase C-lambdaProto-Oncogene Proteins c-akt

Identifiers

PMID19549684
PMCPMC2704884
OpenAlexW1983329226

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.