Evidence map›Paper›PMID 29104065›Full record

ArticleCell chemical biology2018

Design and Profiling of a Subcellular Targeted Optogenetic cAMP-Dependent Protein Kinase.

Colin P O'Banion, Melanie A Priestman, Robert M Hughes, Laura E Herring, Stephen J Capuzzi, David S Lawrence

Open access · bronzeAbstract read
In one paragraph

Article in Cell chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 38 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Colin P O'BanionDivision of Chemical Biology and Medicinal Chemistry, UNC Eshelman School of Pharmacy, University of North Carolina, Chapel Hill, NC 27599, USA.
Melanie A PriestmanDivision of Chemical Biology and Medicinal Chemistry, UNC Eshelman School of Pharmacy, University of North Carolina, Chapel Hill, NC 27599, USA.
Robert M HughesDivision of Chemical Biology and Medicinal Chemistry, UNC Eshelman School of Pharmacy, University of North Carolina, Chapel Hill, NC 27599, USA; Department of Chemistry; East Carolina University, Greenville, NC 27858, USA.
Laura E HerringUNC Proteomics Core, Department of Pharmacology, UNC School of Medicine, University of North Carolina, Chapel Hill, NC 27599, USA.
Stephen J CapuzziDivision of Chemical Biology and Medicinal Chemistry, UNC Eshelman School of Pharmacy, University of North Carolina, Chapel Hill, NC 27599, USA.
David S LawrenceDivision of Chemical Biology and Medicinal Chemistry, UNC Eshelman School of Pharmacy, University of North Carolina, Chapel Hill, NC 27599, USA; Department of Chemistry, University of North Carolina, Chapel Hill, NC 27599, USA; Department of Pharmacology, University of North Carolina, Chapel Hill, NC 27599, USA. Electronic address: lawrencd@email.unc.edu.
University of North Carolina at Chapel Hill · US

Funding

Drug Repurposing for Cancer Therapy: From Man to Molecules to ManU01CA207160 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI TROPSHA, ALEXANDER · 2016 to 2018
$1.2M
Optogenetic Mitochondria-Directed ProteinsR21NS093617 · NINDS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI LAWRENCE, DAVID S. · 2015 to 2016
$418k
NCI NIH HHS U01 CA207160NINDS NIH HHS R21 NS093617
6 · The paper itself

Abstract

Although the cAMP-dependent protein kinase (PKA) is ubiquitously expressed, it is sequestered at specific subcellular locations throughout the cell, thereby resulting in compartmentalized cellular signaling that triggers site-specific behavioral phenotypes. We developed a three-step engineering strategy to construct an optogenetic PKA (optoPKA) and demonstrated that, upon illumination, optoPKA migrates to specified intracellular sites. Furthermore, we designed intracellular spatially segregated reporters of PKA activity and confirmed that optoPKA phosphorylates these reporters in a light-dependent fashion. Finally, proteomics experiments reveal that light activation of optoPKA results in the phosphorylation of known endogenous PKA substrates as well as potential novel substrates.

Indexed as

OptogeneticsCyclic AMP-Dependent Protein KinasesHumansMitochondrial MembranesPhosphorylationCyclic AMP-Dependent Protein KinasescAMP dependent protein kinasecompartmentalized signallingoptogeneticsprotein engineeringprotein kinasesproteomicssynthetic biology

Identifiers

PMID29104065
PMCPMC5777159
OpenAlexW2766215052

What OpenQuestion holds

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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.