Evidence map›Paper›PMID 35959460›Full record

ReviewFrontiers in molecular biosciences2022

Protein Kinase A in cellular migration-Niche signaling of a ubiquitous kinase.

Kathryn V Svec, Alan K Howe

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

6 citing papers in PubMed, 13 citations in OpenAlex.

  1. Nurr1 Orchestrates Claustrum Development and Functionality.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. Rab32 regulates Golgi structure and cell migration through Protein Kinase A-mediated phosphorylation of Optineurin.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Review
  5. The focal adhesion protein talin is a mechanically gated A-kinase anchoring protein.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. 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.

Kathryn V SvecDepartment of Pharmacology, University of Vermont, Burlington, VT, United States.
Alan K HoweDepartment of Pharmacology, University of Vermont, Burlington, VT, United States.
University of Vermont · US

Funding

Mechano-Chemical Regulation of GPCR/PKA Signaling During Cell MigrationR01GM117490 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI HOWE, ALAN K · 2016 to 2019
$1.6M
Protein Kinase A in Focal Adhesions - Mechanisms and ConsequencesR01GM137611 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI HOWE, ALAN K · 2021 to 2022
$747k
NIGMS NIH HHS R01 GM117490NIGMS NIH HHS R01 GM137611
6 · The paper itself

Abstract

Cell migration requires establishment and maintenance of directional polarity, which in turn requires spatial heterogeneity in the regulation of protrusion, retraction, and adhesion. Thus, the signaling proteins that regulate these various structural processes must also be distinctly regulated in subcellular space. Protein Kinase A (PKA) is a ubiquitous serine/threonine kinase involved in innumerable cellular processes. In the context of cell migration, it has a paradoxical role in that global inhibition or activation of PKA inhibits migration. It follows, then, that the subcellular regulation of PKA is key to bringing its proper permissive and restrictive functions to the correct parts of the cell. Proper subcellular regulation of PKA controls not only when and where it is active but also specifies the targets for that activity, allowing the cell to use a single, promiscuous kinase to exert distinct functions within different subcellular niches to facilitate cell movement. In this way, understanding PKA signaling in migration is a study in context and in the elegant coordination of distinct functions of a single protein in a complex cellular process.

Indexed as

cell migrationcompartmentalizationion channelsleading edgeprotein kinase ARho GTPasessubcellular signalingtyrosine kinases

Identifiers

PMID35959460
PMCPMC9361040
OpenAlexW4287960605

What Socratic 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 Socratic graph.