Evidence map›Paper›PMID 31227593›Full record

ArticleThe Journal of cell biology2019

LTK is an ER-resident receptor tyrosine kinase that regulates secretion.

Federica G Centonze, Veronika Reiterer, Karsten Nalbach, Kota Saito, Krzysztof Pawlowski, Christian Behrends, Hesso Farhan

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

32 citing papers in PubMed, 63 citations in OpenAlex.

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  16. Sorting and Export of Proteins at the Endoplasmic Reticulum.Cold Spring Harbor perspectives in biology · 2023
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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

7 authors at 4 institutions in 5 countries.

Federica G CentonzeDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
Veronika ReitererDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
Karsten NalbachMunich Cluster for Systems Neurology, Medical Faculty, Ludwig-Maximilians-Universität München, Munich, Germany.
Kota SaitoDepartment of Biological Informatics and Experimental Therapeutics, Graduate School of Medicine, Akita University, Akita, Japan.ORCID 0000-0003-2478-2687
Krzysztof PawlowskiDepartment of Experimental Design and Bioinformatics, Warsaw University of Life Sciences, Warsaw, Poland.ORCID 0000-0002-5367-0935
Christian BehrendsMunich Cluster for Systems Neurology, Medical Faculty, Ludwig-Maximilians-Universität München, Munich, Germany.
Hesso FarhanDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway hesso.farhan@medisin.uio.no.ORCID 0000-0002-0889-8463
University of Oslo · NOMunich Cluster for Systems Neurology · DEAkita University · JPWarsaw University of Life Sciences · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The endoplasmic reticulum (ER) is a key regulator of cellular proteostasis because it controls folding, sorting, and degradation of secretory proteins. Much has been learned about how environmentally triggered signaling pathways regulate ER function, but only little is known about local signaling at the ER. The identification of ER-resident signaling molecules will help gain a deeper understanding of the regulation of ER function and thus of proteostasis. Here, we show that leukocyte tyrosine kinase (LTK) is an ER-resident receptor tyrosine kinase. Depletion of LTK as well as its pharmacologic inhibition reduces the number of ER exit sites and slows ER-to-Golgi transport. Furthermore, we show that LTK interacts with and phosphorylates Sec12. Expression of a phosphoablating mutant of Sec12 reduces the efficiency of ER export. Thus, LTK-to-Sec12 signaling represents the first example of an ER-resident signaling module with the potential to regulate proteostasis.

Indexed as

Cell LineEndoplasmic ReticulumGuanine Nucleotide Exchange FactorsHumansPhosphorylationProtein BindingProtein DomainsProtein TransportReceptor Protein-Tyrosine KinasesSubcellular FractionsGuanine Nucleotide Exchange FactorsLTK protein, humanReceptor Protein-Tyrosine Kinases

Identifiers

PMID31227593
PMCPMC6683734
OpenAlexW2953305792

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.