Evidence map›Paper›PMID 24500718›Full record

ArticleThe Journal of biological chemistry2014

Protein kinase Cδ-mediated phosphorylation of Connexin43 gap junction channels causes movement within gap junctions followed by vesicle internalization and protein degradation.

Angela C Cone, Gabriel Cavin, Cinzia Ambrosi, Hiroyuki Hakozaki, Alyssa X Wu-Zhang, Maya T Kunkel, Alexandra C Newton, Gina E Sosinsky

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. CD38/ADP-ribose/TRPM2-mediated nuclear CaExperimental & molecular medicine · 2023
    Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Astroglial Connexin43 as a Potential Target for a Mood Stabiliser.International journal of molecular sciences · 2020
    Review
  14. Observational
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Protein⁻Protein Interactions with Connexin 43: Regulation and Function.International journal of molecular sciences · 2018
    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

8 authors at 1 institution in 1 country.

Angela C ConeFrom the National Center for Microscopy and Imaging Research.
Gabriel Cavin
Cinzia Ambrosi
Hiroyuki Hakozaki
Alyssa X Wu-Zhang
Maya T Kunkel
Alexandra C Newton
Gina E Sosinsky
University of California, San Diego · US

Funding

Project# 4: INTERACTIONS OF ANCHORING PROTEINS WITH THEIR TARGETSP01DK054441 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, SUSAN S. · 1999 to 2017
$27.3M
IVEM and Image Analysis ResourceP41GM103412 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ELLISMAN, MARK H · 2012 to 2019
$17.9M
Structure, Function and Regulation of Protein Kinase CR37GM043154 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI NEWTON, ALEXANDRA C. · 2003 to 2012
$4.0M
STRUCTURE AND DYNAMICS OF CONNEXIN26 GAP JUNCTIONSR01GM065937 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PERKINS, GUY A · 2003 to 2016
$3.9M
STRUCTURAL ANALYSIS OF GAP JUNCTION TRAFFICKINGR01GM072881 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PERKINS, GUY A · 2005 to 2015
$2.6M
STRUCTURE/FUNCTION AND REGULATION OF PROTEIN KINASE CR01GM043154 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI NEWTON, ALEXANDRA C. · 1990 to 2016
$2.5M
NIDDK NIH HHS P01 DK054441NIGMS NIH HHS GM043154NIGMS NIH HHS GM072881NIGMS NIH HHS GM103412NIGMS NIH HHS P41 GM103412NIGMS NIH HHS R01 GM043154NIGMS NIH HHS R01 GM065937NIGMS NIH HHS R01 GM072881NIGMS NIH HHS R37 GM043154
6 · The paper itself

Abstract

Phosphorylation of gap junction proteins, connexins, plays a role in global signaling events involving kinases. Connexin43 (Cx43), a ubiquitous and important connexin, has several phosphorylation sites for specific kinases. We appended an imaging reporter tag for the activity of the δ isoform of protein kinase C (PKCδ) to the carboxyl terminus of Cx43. The FRET signal of this reporter is inversely related to the phosphorylation of serine 368 of Cx43. By activating PKC with the phorbol ester phorbol 12,13-dibutyrate (PDBu) or a natural stimulant, UTP, time lapse live cell imaging movies indicated phosphorylated Ser-368 Cx43 separated into discrete domains within gap junctions and was internalized in small vesicles, after which it was degraded by lysosomes and proteasomes. Mutation of Ser-368 to an Ala eliminated the response to PDBu and changes in phosphorylation of the reporter. A phosphatase inhibitor, calyculin A, does not change this pattern, indicating PKC phosphorylation causes degradation of Cx43 without dephosphorylation, which is in accordance with current hypotheses that cells control their intercellular communication by a fast and constant turnover of connexins, using phosphorylation as part of this mechanism.

Indexed as

MovementProteolysisAnimalsChlorocebus aethiopsConnexin 43COS CellsGap JunctionsHeLa CellsHumansPhorbol EstersPhosphoric Monoester HydrolasesPhosphorylationProtein Kinase C-deltaProtein Kinase InhibitorsProtein TransportSerineConnexin 43Phorbol EstersPhosphoric Monoester HydrolasesProtein Kinase C-deltaProtein Kinase InhibitorsSerineCell JunctionsConnexinGap JunctionsHemichannelsIntercellular CommunicationMembrane Protein DegradationMembrane Protein TraffickingProtein Kinase C (PKC)Protein Phosphorylation

Identifiers

PMID24500718
PMCPMC3979370
OpenAlexW2054859999

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.