Evidence map›Paper›PMID 15491280›Full record

ReviewThe Biochemical journal2004

Distinctive activation mechanisms and functions for protein kinase Cdelta.

Susan F Steinberg

Open access · bronzeAbstract readReview
In one paragraph

Review in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 167 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
167citing papers in PubMed, 1 pooled it
10.6field-weighted citation impact, top 1% 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

167 citing papers in PubMed, 1 synthesis or guideline pooled it, 372 citations in OpenAlex.

  1. Pooled it
  2. Review
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  15. 12-Cells · 2022
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107 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Susan F SteinbergDepartment of Pharmacology, College of Physicians and Surgeons, Columbia University, 630 West 168 Street, New York, NY 10032, USA. sfs1@columbia.edu
Columbia University · US

Funding

Protein kinase C-delta actions in cardiomyocytesR01HL077860 · NHLBI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI STEINBERG, SUSAN F · 2004 to 2013
$3.4M
PROTEASE-ACTIVATED RECEPTOR ACTIONS IN CARDIOMYOCYTESR01HL064639 · NHLBI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI STEINBERG, SUSAN F · 2001 to 2004
$1.5M
NHLBI NIH HHS HL-64639NHLBI NIH HHS HL-77860NHLBI NIH HHS R01 HL064639NHLBI NIH HHS R01 HL077860
6 · The paper itself

Abstract

PKCdelta (protein kinase Cdelta) is a serine/threonine kinase that plays a key role in growth regulation and tissue remodelling. Traditional models of PKC activation have focused on lipid cofactors and anchoring proteins that localize the active conformation of PKCdelta to membranes, in close proximity with its target substrates. However, recent studies identify a distinct mode for PKCdelta activation involving tyrosine phosphorylation by Src family kinases. The tyrosine-phosphorylated form of PKCdelta (which accumulates in the soluble fraction of cells exposed to oxidant stress) displays lipid-independent kinase activity and is uniquely positioned to phosphorylate target substrates throughout the cell (not just on lipid membranes). This review summarizes (1) recent progress towards understanding structure-activity relationships for PKCdelta, with a particular focus on the stimuli that induce (and the distinct functional consequences that result from) tyrosine phosphorylation events in PKCdelta's regulatory, hinge and catalytic domains; (2) current concepts regarding the role of tyrosine phosphorylation as a mechanism to regulate PKCdelta localization and actions in mitochondrial and nuclear compartments; and (3) recent literature delineating distinct roles for PKCdelta (relative to other PKC isoforms) in transcriptional regulation, cell cycle progression and programmed cell death (including studies in PKCdelta-/- mice that implicate PKCdelta in immune function and cardiovascular remodelling). Collectively, these studies argue that the conventional model for PKCdelta activation must be broadened to allow for stimulus-specific differences in PKCdelta signalling during growth factor stimulation and oxidant stress.

Indexed as

AnimalsEnzyme ActivationHumansMyocytes, CardiacPhosphorylationPhosphotyrosineProtein Kinase CProtein Kinase C-deltaSubstrate SpecificityPhosphotyrosinePRKCD protein, humanProtein Kinase CProtein Kinase C-delta

Identifiers

PMID15491280
PMCPMC1134130
OpenAlexW2126681184

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.