Evidence map›Paper›PMID 21454606›Full record

ArticleThe Journal of biological chemistry2011

Phosphorylation of connexin 50 by protein kinase A enhances gap junction and hemichannel function.

Jialu Liu, Jose F Ek Vitorin, Susan T Weintraub, Sumin Gu, Qian Shi, Janis M Burt, Jean X Jiang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

31 citing papers in PubMed, 50 citations in OpenAlex.

  1. Deceiving the gatekeepers: virus modulation of gap junctions.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Mechanisms of Connexin Regulating Peptides.International journal of molecular sciences · 2021
    Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Connexin channel and its role in diabetic retinopathy.Progress in retinal and eye research · 2017
    Review
  15. Review
  16. Article
  17. Focus on lens connexins.BMC cell biology · 2017
    Review
  18. Article
  19. Review
  20. 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

7 authors at 2 institutions in 1 country.

Jialu LiuDepartment of Biochemistry, University of Texas Health Science Center, San Antonio, Texas 78229, USA.
Jose F Ek Vitorin
Susan T Weintraub
Sumin Gu
Qian Shi
Janis M Burt
Jean X Jiang
The University of Texas Health Science Center at San Antonio · USUniversity of Arizona · US

Funding

Intercellular Communication in the Eye LensR01EY012085 · NEI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Jean X Jiang · 2003 to 2026
$8.4M
INTERCELLULAR COMMUNICATION IN THE EYE LENSR29EY012085 · NEI · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI JIANG, JEAN X · 1998 to 2002
$312k
NEI NIH HHS EY012085NEI NIH HHS R01 EY012085NEI NIH HHS R29 EY012085
6 · The paper itself

Abstract

Phosphorylation of connexins is an important mechanism regulating gap junction channels. However, the role(s) of connexin (Cx) phosphorylation in vivo are largely unknown. Here, we showed by mass spectrometry that Ser-395 in the C terminus of chicken Cx50 was phosphorylated in the lens. Ser-395 is located within a PKA consensus site. Analyses of Cx50 phosphorylation by two-dimensional thin layer chromatography tryptic phosphopeptide profiles suggested that Ser-395 was targeted by PKA in vivo. PKA activation increased both gap junction dye coupling and hemichannel dye uptake in a manner not involving increases in total Cx50 expression or relocation to the cell surface or gap junctional plaques. Single channel recordings indicated PKA enhanced transitions between the closed and ∼200-pS open state while simultaneously reducing transitions between this open state and a ∼65-pS subconductance state. The mutation of Ser-395 to alanine significantly attenuated PKA-induced increases in dye coupling and uptake by Cx50. However, channel records indicated that phosphorylation at this site was unnecessary for enhanced transitions between the closed and ∼200-pS conductance state. Together, these results suggest that Cx50 is phosphorylated in vivo by PKA at Ser-395 and that this event, although unnecessary for PKA-induced alterations in channel conductance, promotes increased dye permeability of Cx50 channels, which plays an important role in metabolic coupling and transport in lens fibers.

Indexed as

AnimalsCell MembraneChick EmbryoChromatography, High Pressure LiquidChromatography, Thin LayerConnexin 50ConnexinsCyclic AMP-Dependent Protein KinasesEye ProteinsGap JunctionsMass SpectrometryPhosphopeptidesPhosphorylationRecombinant ProteinsSerineSpectrometry, Mass, Electrospray IonizationConnexin 50ConnexinsCyclic AMP-Dependent Protein KinasesEye ProteinsPhosphopeptidesRecombinant ProteinsSerineTrypsin

Identifiers

PMID21454606
PMCPMC3089535
OpenAlexW2011664297

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.