Evidence map›Paper›PMID 35361526›Full record

ReviewTrends in biochemical sciences2022

Protein kinase C: release from quarantine by mTORC2.

Timothy R Baffi, Alexandra C Newton

Open access · greenAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

15 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Making PI3K superfamily enzymes run faster.Advances in biological regulation · 2025
    Review
  8. Article
  9. Endocannabinoid biosynthetic enzymes regulate pain response via LKB1-AMPK signaling.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
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 2 institutions in 1 country.

Timothy R BaffiDepartment of Pharmacology, University of California at San Diego, La Jolla, CA 92093, USA; Division of Signaling and Gene Expression, La Jolla Institute for Immunology, La Jolla, CA 92093, USA; Sanford Consortium for Regenerative Medicine, La Jolla, CA 92093, USA.
Alexandra C NewtonDepartment of Pharmacology, University of California at San Diego, La Jolla, CA 92093, USA. Electronic address: anewton@health.ucsd.edu.
La Jolla Institute for Immunology · USUniversity of California San Diego · US

Funding

Molecular Mechanisms of Cell SignalingR35GM122523 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ALEXANDRA C. NEWTON · 2017 to 2026
$6.7M
NIGMS NIH HHS R35 GM122523
6 · The paper itself

Abstract

Protein kinase C (PKC) isozymes are maintained in a 'ready-to-go' but 'safe' autoinhibited conformation until second messenger binding unleashes an autoinhibitory pseudosubstrate to allow substrate phosphorylation. However, to gain this 'ready-to-go' conformation, PKC must be processed by a series of complex priming phosphorylations, the mechanism of which was enigmatic until now. Recent findings snapped the pieces of the phosphorylation puzzle into place to unveil a process that involves a newly described motif (TOR interaction motif, TIM), a well-described kinase [mechanistic target of rapamycin complex 2 (mTORC2)], and an often-used mechanism (autophosphorylation) to prime PKC to signal. This review highlights new insights into how phosphorylation controls PKC and discusses them in the context of common mechanisms for AGC kinase regulation by phosphorylation and autophosphorylation.

Indexed as

Protein Kinase CQuarantineIsoenzymesMechanistic Target of Rapamycin Complex 2PhosphorylationIsoenzymesMechanistic Target of Rapamycin Complex 2Protein Kinase CautophosphorylationmTORC2phosphorylationPKC

Identifiers

PMID35361526
PMCPMC10936736
OpenAlexW4220996952

What OpenQuestion holds

Textmetadata
LicenceTDM
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.