Evidence map›Paper›PMID 29572475›Full record

ArticleNature communications2018

Structure and evolution of the Fam20 kinases.

Hui Zhang, Qinyu Zhu, Jixin Cui, Yuxin Wang, Mark J Chen, Xing Guo, Vincent S Tagliabracci, Jack E Dixon, Junyu Xiao

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

46 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
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  12. Article
  13. KINtaro: protein kinase-like database.BMC research notes · 2024
    Article
  14. Frontiers in immunology · 2024
    Article
  15. Deficiency ofInternational journal of molecular sciences · 2023
    Article
  16. Emerging functions of pseudoenzymes.The Biochemical journal · 2023
    Review
  17. Review
  18. Review
  19. Article
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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

9 authors at 5 institutions in 2 countries.

Hui ZhangThe State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking-Tsinghua Center for Life Sciences, Peking University, 100871, Beijing, China.
Qinyu ZhuThe State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking-Tsinghua Center for Life Sciences, Peking University, 100871, Beijing, China.
Jixin CuiDepartment of Pharmacology, University of California, San Diego, La Jolla, CA, 92093, USA.
Yuxin WangThe State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking-Tsinghua Center for Life Sciences, Peking University, 100871, Beijing, China.
Mark J ChenDepartment of Pathology, St. Jude Children's Research Hospital, Memphis, TN, 38015, USA.ORCID http://orcid.org/0000-0003-1169-563X
Xing GuoThe Life Sciences Institute, Zhejiang University, 310058, Hangzhou, China.
Vincent S TagliabracciDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX, 75390, USA.
Jack E DixonDepartment of Pharmacology, University of California, San Diego, La Jolla, CA, 92093, USA.
Junyu XiaoThe State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking-Tsinghua Center for Life Sciences, Peking University, 100871, Beijing, China. junyuxiao@pku.edu.cn.ORCID http://orcid.org/0000-0003-1822-1701
Peking University · CNUniversity of California San Diego · USSt. Jude Children's Research Hospital · USThe University of Texas Southwestern Medical Center · USZhejiang University · CN

Funding

REGULATION OF NEUROPEPTIDE BIOSYNTHESISR01DK018849 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI DIXON, JACK E, WORBY, CAROLYN ANN · 1986 to 2020
$7.0M
STUDIES ON PANCREATIC HORMONESR01DK018024 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DIXON, JACK E, WORBY, CAROLYN ANN · 1986 to 2018
$2.1M
Phosphorylation of FGF23 coordinates crosstalk between the skeleton and kidneyR00DK099254 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI TAGLIABRACCI, VINCENT SCOTT · 2015 to 2017
$746k
NIDDK NIH HHS R00 DK099254NIDDK NIH HHS R01 DK018024NIDDK NIH HHS R01 DK018849
6 · The paper itself

Abstract

The Fam20 proteins are novel kinases that phosphorylate secreted proteins and proteoglycans. Fam20C phosphorylates hundreds of secreted proteins and is activated by the pseudokinase Fam20A. Fam20B phosphorylates a xylose residue to regulate proteoglycan synthesis. Despite these wide-ranging and important functions, the molecular and structural basis for the regulation and substrate specificity of these kinases are unknown. Here we report molecular characterizations of all three Fam20 kinases, and show that Fam20C is activated by the formation of an evolutionarily conserved homodimer or heterodimer with Fam20A. Fam20B has a unique active site for recognizing Galβ1-4Xylβ1, the initiator disaccharide within the tetrasaccharide linker region of proteoglycans. We further show that in animals the monomeric Fam20B preceded the appearance of the dimeric Fam20C, and the dimerization trait of Fam20C emerged concomitantly with a change in substrate specificity. Our results provide comprehensive structural, biochemical, and evolutionary insights into the function of the Fam20 kinases.

Indexed as

AnimalsCasein Kinase ICatalytic DomainCrystallography, X-RayExtracellular Matrix ProteinsHumansHydrogen BondingInsectaMutationPhosphorylationPhosphotransferases (Alcohol Group Acceptor)PhylogenyPolysaccharidesProtein MultimerizationProteoglycansSubstrate SpecificityCasein Kinase IExtracellular Matrix ProteinsFAM20B protein, humanFAM20C protein, humanPhosphotransferases (Alcohol Group Acceptor)PolysaccharidesProteoglycansXylose

Identifiers

PMID29572475
PMCPMC5865150
OpenAlexW2792567205

What OpenQuestion holds

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Registered trials

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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.