Evidence map›Paper›PMID 25789606›Full record

ArticleeLife2015

A secretory kinase complex regulates extracellular protein phosphorylation.

Jixin Cui, Junyu Xiao, Vincent S Tagliabracci, Jianzhong Wen, Meghdad Rahdar, Jack E Dixon

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
11.0field-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

87 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Functions of secretory calcium-binding phosphoproteins in dental mineralization.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2025
    Review
  9. Review
  10. Review
  11. Article
  12. Mechanisms of assembly and remodelling of the extracellular matrix.Nature reviews. Molecular cell biology · 2024
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Frontiers in immunology · 2024
    Article
  18. Article
  19. Emerging functions of pseudoenzymes.The Biochemical journal · 2023
    Review
  20. Review

27 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Jixin CuiDepartment of Pharmacology, University of California, San Diego, La Jolla, United States.
Junyu XiaoDepartment of Pharmacology, University of California, San Diego, La Jolla, United States.
Vincent S TagliabracciDepartment of Pharmacology, University of California, San Diego, La Jolla, United States.
Jianzhong WenDepartment of Pharmacology, University of California, San Diego, La Jolla, United States.
Meghdad RahdarDepartment of Pharmacology, University of California, San Diego, La Jolla, United States.
Jack E DixonDepartment of Pharmacology, University of California, San Diego, La Jolla, United States.
University of California, San Diego · US

Funding

STUDIES ON PANCREATIC HORMONESR37DK018024 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI DIXON, JACK E · 1988 to 2013
$5.6M
STUDIES ON PANCREATIC HORMONESR01DK018024 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DIXON, JACK E, WORBY, CAROLYN ANN · 1986 to 2018
$2.1M
NIDDK NIH HHS R01 DK018024
6 · The paper itself

Abstract

Although numerous extracellular phosphoproteins have been identified, the protein kinases within the secretory pathway have only recently been discovered, and their regulation is virtually unexplored. Fam20C is the physiological Golgi casein kinase, which phosphorylates many secreted proteins and is critical for proper biomineralization. Fam20A, a Fam20C paralog, is essential for enamel formation, but the biochemical function of Fam20A is unknown. Here we show that Fam20A potentiates Fam20C kinase activity and promotes the phosphorylation of enamel matrix proteins in vitro and in cells. Mechanistically, Fam20A is a pseudokinase that forms a functional complex with Fam20C, and this complex enhances extracellular protein phosphorylation within the secretory pathway. Our findings shed light on the molecular mechanism by which Fam20C and Fam20A collaborate to control enamel formation, and provide the first insight into the regulation of secretory pathway phosphorylation.

Indexed as

AmeloblastsAmino Acid SequenceAnimalsCasein Kinase ICell LineDental Enamel ProteinsExtracellular Matrix ProteinsFemaleFounder EffectGene ExpressionGene Expression RegulationHumansLepidopteraMammary Glands, AnimalMiceMice, Inbred C57BLCasein Kinase IDental Enamel Proteinsenamel matrix proteinsExtracellular Matrix ProteinsFAM20A protein, humanFAM20C protein, humanRecombinant Proteinsbiochemistryextracellular protein phosphorylationhumankinase complexmousepseudokinasesecretory pathway phosphorylationtooth enamel formation

Identifiers

PMID25789606
PMCPMC4421793
OpenAlexW2109825944

What OpenQuestion 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 OpenQuestion graph.