Evidence map›Paper›PMID 26739752›Full record

ArticleMolecular biology of the cell2016

Differential regulation of translation and endocytosis of alternatively spliced forms of the type II bone morphogenetic protein (BMP) receptor.

Ayelet R Amsalem, Barak Marom, Keren E Shapira, Tal Hirschhorn, Livia Preisler, Pia Paarmann, Petra Knaus, Yoav I Henis, Marcelo Ehrlich

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 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 16% 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, 19 citations in OpenAlex.

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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 2 institutions in 2 countries.

Ayelet R AmsalemDepartment of Neurobiology, Tel Aviv University, Tel Aviv 69978, Israel.
Barak MaromDepartment of Neurobiology, Tel Aviv University, Tel Aviv 69978, Israel.
Keren E ShapiraDepartment of Neurobiology, Tel Aviv University, Tel Aviv 69978, Israel.
Tal HirschhornDepartment of Cell Research and Immunology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel.
Livia PreislerDepartment of Neurobiology, Tel Aviv University, Tel Aviv 69978, Israel.
Pia PaarmannInstitute for Chemistry and Biochemistry, Freie Univesitaet Berlin, 1495 Berlin, Germany.
Petra KnausInstitute for Chemistry and Biochemistry, Freie Univesitaet Berlin, 1495 Berlin, Germany.
Yoav I HenisDepartment of Neurobiology, Tel Aviv University, Tel Aviv 69978, Israel henis@post.tau.ac.il marceloe@post.tau.ac.il.
Marcelo EhrlichDepartment of Cell Research and Immunology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel henis@post.tau.ac.il marceloe@post.tau.ac.il.
Tel Aviv University · ILFreie Universität Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The expression and function of transforming growth factor-β superfamily receptors are regulated by multiple molecular mechanisms. The type II BMP receptor (BMPRII) is expressed as two alternatively spliced forms, a long and a short form (BMPRII-LF and -SF, respectively), which differ by an ∼500 amino acid C-terminal extension, unique among TGF-β superfamily receptors. Whereas this extension was proposed to modulate BMPRII signaling output, its contribution to the regulation of receptor expression was not addressed. To map regulatory determinants of BMPRII expression, we compared synthesis, degradation, distribution, and endocytic trafficking of BMPRII isoforms and mutants. We identified translational regulation of BMPRII expression and the contribution of a 3' terminal coding sequence to this process. BMPRII-LF and -SF differed also in their steady-state levels, kinetics of degradation, intracellular distribution, and internalization rates. A single dileucine signal in the C-terminal extension of BMPRII-LF accounted for its faster clathrin-mediated endocytosis relative to BMPRII-SF, accompanied by mildly faster degradation. Higher expression of BMPRII-SF at the plasma membrane resulted in enhanced activation of Smad signaling, stressing the potential importance of the multilayered regulation of BMPRII expression at the plasma membrane.

Indexed as

Alternative SplicingEndocytosisProtein BiosynthesisAnimalsBone Morphogenetic Protein Receptors, Type IICell MembraneChlorocebus aethiopsClathrin-Coated VesiclesCOS CellsGene Expression RegulationHEK293 CellsHumansMutationProtein IsoformsProteolysisReceptors, Transforming Growth Factor betaBMPR2 protein, humanBone Morphogenetic Protein Receptors, Type IIProtein IsoformsReceptors, Transforming Growth Factor betaSmad Proteins, Receptor-Regulated

Identifiers

PMID26739752
PMCPMC4750929
OpenAlexW2259586517

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.