Evidence map›Paper›PMID 25172423›Full record

ArticleCellular signalling2014

cGMP-dependent protein kinase I gamma encodes a nuclear localization signal that regulates nuclear compartmentation and function.

Jingsi Chen, Jesse D Roberts

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cellular signalling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Lysyl oxidase regulation and protein aldehydes in the injured newborn lung.American journal of physiology. Lung cellular and molecular physiology · 2022
    Article
  3. cGMP-dependent protein kinase I in vascular smooth muscle cells improves ischemic stroke outcome in mice.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2019
    Article
  4. Article
  5. 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

2 authors at 1 institution in 1 country.

Jingsi ChenCardiovascular Research Center, Massachusetts General Hospital, Boston, MA, USA; Harvard Medical School, Cambridge, MA, USA.
Jesse D RobertsCardiovascular Research Center, Massachusetts General Hospital, Boston, MA, USA; Harvard Medical School, Cambridge, MA, USA; Departments of Anesthesia, Pediatrics, Massachusetts General Hospital, Boston, MA, USA; Department of Medicine, Massachusetts General Hospital, Boston, MA, USA. Electronic address: roberts@cvrc.mgh.harvard.edu.
Harvard University · US

Funding

Mechanisms regulating PKGI proteolysis and modulation of pulmonary SMC phenotypeR01HL096779 · NHLBI · MASSACHUSETTS GENERAL HOSPITAL · PI ROBERTS, JESSE D · 2010 to 2013
$1.7M
NHLBI NIH HHS R01 HL096779NHLBI NIH HHS R01HL096779
6 · The paper itself

Abstract

cGMP-dependent protein kinase I (PKGI) plays an important role in regulating how cGMP specifies vascular smooth muscle cell (SMC) phenotype. Although studies indicate that PKGI nuclear localization controls how cGMP regulates gene expression in SMC, information about the mechanisms that regulate PKGI nuclear compartmentation and its role in directly regulating cell phenotype is limited. Here we characterize a nuclear localization signal sequence (NLS) in PKGIγ, a proteolytically cleaved PKGI kinase fragment that translocates to the nucleus of SMC. Immuno-localization studies using cells expressing native and NLS-mutant PKGIγ, and treated with a small molecule nuclear transport inhibitor, indicated that PKGIγ encodes a constitutively active NLS that requires importin α and β for regulation of its compartmentation. Moreover, studies utilizing a genetically encoded nuclear phospho-CREB biosensor probe and fluorescence lifetime imaging microscopy demonstrated that this NLS controls PKGIγ nuclear function. In addition, although cytosolic PKGIγ-activity was observed to stimulate MAPK/ERK-mediated nuclear CREB signaling in SMC, NLS-mediated PKGIγ nuclear activity alone was determined to increase the expression of differentiation marker proteins in these cells. These results indicate that NLS-mediated nuclear PKGIγ localization plays an important role in how PKGI regulates vascular SMC phenotype.

Indexed as

AnimalsBiological TransportCell DifferentiationCell LineCell NucleusCyclic AMP Response Element-Binding ProteinCyclic GMP-Dependent Protein Kinase Type IFibroblastsMAP Kinase Signaling SystemMitogen-Activated Protein KinasesMuscle, Smooth, VascularMyocytes, Smooth MuscleNuclear Localization SignalsNuclear ProteinsRatsCyclic AMP Response Element-Binding ProteinCyclic GMP-Dependent Protein Kinase Type IMitogen-Activated Protein KinasesNuclear Localization SignalsNuclear ProteinscGMP-dependent protein kinasecGMP signal transductionNuclear translocationSmooth muscle cell

Identifiers

PMID25172423
PMCPMC4254301
OpenAlexW2020618262

What OpenQuestion holds

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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.