Evidence map›Paper›PMID 34349020›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Proteolytic processing of secretory pathway kinase Fam20C by site-1 protease promotes biomineralization.

Xinxin Chen, Jianchao Zhang, Pulan Liu, Yangyang Wei, Xi'e Wang, Junyu Xiao, Chih-Chen Wang, Lei Wang

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 35 citations in OpenAlex.

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  8. Structural basis for substrate selectivity by site-one protease revealed by studies with a small-molecule inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

8 authors at 2 institutions in 1 country.

Xinxin ChenNational Laboratory of Biomacromolecules, Chinese Academy of Sciences (CAS) Center for Excellence in Biomacromolecules, Institute of Biophysics, CAS, Beijing 100101, China.ORCID 0000-0002-4766-8169
Jianchao ZhangNational Laboratory of Biomacromolecules, Chinese Academy of Sciences (CAS) Center for Excellence in Biomacromolecules, Institute of Biophysics, CAS, Beijing 100101, China.
Pulan LiuThe State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, China.
Yangyang WeiThe State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, China.ORCID 0000-0002-2363-4941
Xi'e WangNational Laboratory of Biomacromolecules, Chinese Academy of Sciences (CAS) Center for Excellence in Biomacromolecules, Institute of Biophysics, CAS, Beijing 100101, China.
Junyu XiaoThe State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, China.ORCID 0000-0003-1822-1701
Chih-Chen WangNational Laboratory of Biomacromolecules, Chinese Academy of Sciences (CAS) Center for Excellence in Biomacromolecules, Institute of Biophysics, CAS, Beijing 100101, China.
Lei WangNational Laboratory of Biomacromolecules, Chinese Academy of Sciences (CAS) Center for Excellence in Biomacromolecules, Institute of Biophysics, CAS, Beijing 100101, China; wanglei@ibp.ac.cn.ORCID 0000-0002-5071-5800
Chinese Academy of Sciences · CNPeking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Family with sequence similarity 20C (Fam20C), the major protein kinase in the secretory pathway, generates the vast majority of the secreted phosphoproteome. However, the regulatory mechanisms of Fam20C transport, secretion, and function remain largely unexplored. Here, we show that Fam20C exists as a type II transmembrane protein within the secretory compartments, with its N-terminal signal peptide-like region serving as a membrane anchor for Golgi retention. The secretion and kinase activity of Fam20C are governed by site-1 protease (S1P), a key regulator of cholesterol homeostasis. We find that only mature Fam20C processed by S1P functions in osteoblast differentiation and mineralization. Together, our findings reveal a unique mechanism for Fam20C secretion and activation via proteolytic regulation, providing a molecular link between biomineralization and lipid metabolism.

Indexed as

Amino Acid MotifsAnimalsCalcium-Binding ProteinsCasein Kinase ICell DifferentiationCOP-Coated VesiclesExtracellular Matrix ProteinsGolgi ApparatusHeLa CellsHumansMiceMutationOsteoblastsProprotein ConvertasesProtein DomainsProtein TransportCalcium-Binding ProteinsCasein Kinase IExtracellular Matrix ProteinsFAM20C protein, humanFAM20C protein, mousemembrane-bound transcription factor peptidase, site 1PF-429242Proprotein ConvertasesPyrrolidinesSerine EndopeptidasesFam20CGolgiphosphorylationproteolysissite-1 protease

Identifiers

PMID34349020
PMCPMC8364200
OpenAlexW3189330738

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.