Evidence map›Paper›PMID 29158294›Full record

ArticleMolecular and cellular biology2018

The Actin-Binding Protein PPP1r18 Regulates Maturation, Actin Organization, and Bone Resorption Activity of Osteoclasts.

Takuma Matsubara, Shoichiro Kokabu, Chihiro Nakatomi, Masayuki Kinbara, Toshihiro Maeda, Mitsuhiro Yoshizawa, Hisataka Yasuda, Teruko Takano-Yamamoto, Roland Baron, Eijiro Jimi

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

13 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
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  7. Tyrosine Kinase Src Is a Regulatory Factor of Bone Homeostasis.International journal of molecular sciences · 2022
    Review
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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

10 authors at 5 institutions in 2 countries.

Takuma MatsubaraDivision of Molecular Signaling and Biochemistry, Department of Health Improvement, Kyushu Dental University, Fukuoka, Japan r15matsubara@fa.kyu-dent.ac.jp.ORCID https://orcid.org/0000-0002-8505-0431
Shoichiro KokabuDivision of Molecular Signaling and Biochemistry, Department of Health Improvement, Kyushu Dental University, Fukuoka, Japan.
Chihiro NakatomiDivision of Molecular Signaling and Biochemistry, Department of Health Improvement, Kyushu Dental University, Fukuoka, Japan.
Masayuki KinbaraDepartment of Orthodontics and Dentofacial Orthopedics, Graduate School of Dentistry, Tohoku University, Sendai, Japan.
Toshihiro MaedaDepartment of Orthodontics and Dentofacial Orthopedics, Graduate School of Dentistry, Tohoku University, Sendai, Japan.
Mitsuhiro YoshizawaDepartment of Orthodontics and Dentofacial Orthopedics, Graduate School of Dentistry, Tohoku University, Sendai, Japan.
Hisataka YasudaNagahama Institute for Biochemical Science, Oriental Yeast Co., Ltd., Shiga, Japan.
Teruko Takano-YamamotoDepartment of Orthodontics and Dentofacial Orthopedics, Graduate School of Dentistry, Tohoku University, Sendai, Japan.
Roland BaronDepartment of Medicine, Harvard Medical School, and Division of Bone and Mineral Research, Department of Oral Medicine, Infection and Immunity, Harvard School of Dental Medicine, Boston, Massachusetts, USA.
Eijiro JimiDivision of Molecular Signaling and Biochemistry, Department of Health Improvement, Kyushu Dental University, Fukuoka, Japan.
Tohoku University · JPKyushu Dental University · JPHarvard University · USKyushu University · JPNagahama Institute of Bio-Science and Technology · JP

Funding

Mechanisms and function of the microtubule podosome connection in osteoclastsR01AR062054 · NIAMS · HARVARD MEDICAL SCHOOL · PI BARON, ROLAND E · 2012 to 2016
$2.8M
NIAMS NIH HHS R01 AR062054
6 · The paper itself

Abstract

Osteoclasts resorb bone by attaching on the bone matrix and forming a sealing zone. In Src-deficient mice, osteoclasts cannot form the actin ring, a characteristic actin structure that seals the resorbed area, and resorb hardly any bone as a result. However, the molecular mechanism underlying the role of Src in the regulation and organization of the actin ring is still unclear. We identified an actin-regulatory protein, protein phosphatase 1 regulatory subunit 18 (PPP1r18), as an Src-binding protein in an Src-, Yes-, and Fyn-deficient fibroblast (SYF) cell line overexpressing a constitutively active form of Src. PPP1r18 was localized in the nucleus and actin ring. PPP1r18 overexpression in osteoclasts inhibited terminal differentiation, actin ring formation, and bone-resorbing activity. A mutation of the protein phosphatase 1 (PP1)-binding domain of PPP1r18 rescued these phenotypes. In contrast, PPP1r18 knockdown promoted terminal differentiation and actin ring formation. In summary, we showed that PPP1r18 likely plays a role in podosome organization and bone resorption.

Indexed as

ActinsAnimalsBone ResorptionCell AdhesionCell DifferentiationCell LineDopamine and cAMP-Regulated Phosphoprotein 32HumansMaleMiceMice, TransgenicOsteoclastsProtein BindingProtein Phosphatase 1Protein-Tyrosine KinasesReceptors, Neuropeptide YActinsDopamine and cAMP-Regulated Phosphoprotein 32neuropeptide Y4 receptorPPP1R1B protein, humanProtein Phosphatase 1Protein-Tyrosine KinasesReceptors, Neuropeptide Ysrc-Family Kinasesbone resorptioncell adhesionosteoclast

Identifiers

PMID29158294
PMCPMC5789032
OpenAlexW2768779521

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.