Evidence map›Paper›PMID 27760174›Full record

ArticlePloS one2016

BAR Proteins PSTPIP1/2 Regulate Podosome Dynamics and the Resorption Activity of Osteoclasts.

Martin Sztacho, Sandra Segeletz, Maria Arantzazu Sanchez-Fernandez, Cornelia Czupalla, Christian Niehage, Bernard Hoflack

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.7field-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

15 citing papers in PubMed, 28 citations in OpenAlex.

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  14. Forces and constraints controlling podosome assembly and disassembly.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019
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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

6 authors at 1 institution in 1 country.

Martin SztachoBiotechnology Center, Technische Universität Dresden, Tatzberg 47-51, 01307, Dresden, Germany.
Sandra SegeletzBiotechnology Center, Technische Universität Dresden, Tatzberg 47-51, 01307, Dresden, Germany.
Maria Arantzazu Sanchez-FernandezBiotechnology Center, Technische Universität Dresden, Tatzberg 47-51, 01307, Dresden, Germany.
Cornelia CzupallaBiotechnology Center, Technische Universität Dresden, Tatzberg 47-51, 01307, Dresden, Germany.
Christian NiehageBiotechnology Center, Technische Universität Dresden, Tatzberg 47-51, 01307, Dresden, Germany.
Bernard HoflackBiotechnology Center, Technische Universität Dresden, Tatzberg 47-51, 01307, Dresden, Germany.
TU Dresden · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bone resorption in vertebrates relies on the ability of osteoclasts to assemble F-actin-rich podosomes that condense into podosomal belts, forming sealing zones. Sealing zones segregate bone-facing ruffled membranes from other membrane domains, and disassemble when osteoclasts migrate to new areas. How podosome/sealing zone dynamics is regulated remains unknown. We illustrate the essential role of the membrane scaffolding F-BAR-Proline-Serine-Threonine Phosphatase Interacting Proteins (PSTPIP) 1 and 2 in this process. Whereas PSTPIP2 regulates podosome assembly, PSTPIP1 regulates their disassembly. PSTPIP1 recruits, through its F-BAR domain, the protein tyrosine phosphatase non-receptor type 6 (PTPN6) that de-phosphophorylates the phosphatidylinositol 5-phosphatases SHIP1/2 bound to the SH3 domain of PSTPIP1. Depletion of any component of this complex prevents sealing zone disassembly and increases osteoclast activity. Thus, our results illustrate the importance of BAR domain proteins in podosome structure and dynamics, and identify a new PSTPIP1/PTPN6/SHIP1/2-dependent negative feedback mechanism that counterbalances Src and PI(3,4,5)P3 signalling to control osteoclast cell polarity and activity during bone resorption.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsBone ResorptionCytoskeletal ProteinsGene Knockout TechniquesHEK293 CellsHumansMiceOsteoclastsPhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPodosomesProtein DomainsProtein Tyrosine Phosphatases, Non-ReceptorProteomicsRAW 264.7 CellsRNA InterferenceAdaptor Proteins, Signal TransducingCytoskeletal ProteinsInpp5d protein, mouseInppl1 protein, mousePhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorPstpip1 protein, mousePstpip2 protein, mouse

Identifiers

PMID27760174
PMCPMC5070766
OpenAlexW2539263579

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.