Evidence map›Paper›PMID 29535802›Full record

ArticleOncotarget2018

The KDEL receptor signalling cascade targets focal adhesion kinase on focal adhesions and invadopodia.

Carmen Ruggiero, Mauro Grossi, Giorgia Fragassi, Antonella Di Campli, Carmine Di Ilio, Alberto Luini, Michele Sallese

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2018. 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
0.9field-weighted citation impact, top 26% 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, 24 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

7 authors at 3 institutions in 2 countries.

Carmen RuggieroCNRS, NEOGENEX CNRS International Associated Laboratory, Institut de Pharmacologie Moléculaire et Cellulaire, Université Côte d'Azur, Sophia Antipolis, Valbonne, France.
Mauro GrossiCNRS, NEOGENEX CNRS International Associated Laboratory, Institut de Pharmacologie Moléculaire et Cellulaire, Université Côte d'Azur, Sophia Antipolis, Valbonne, France.
Giorgia FragassiDepartment of Medicine and Agency Sciences, 'G. d'Annunzio' University of Chieti-Pescara, Regional Health Care Agency of Abruzzo, Pescara, Italy.
Antonella Di CampliInstitute of Protein Biochemistry, National Research Council, Naples, Italy.
Carmine Di IlioDepartment of Medical, Oral and Biotechnological Sciences, 'G. d'Annunzio' University of Chieti-Pescara, Chieti, Italy.
Alberto LuiniInstitute of Protein Biochemistry, National Research Council, Naples, Italy.
Michele SalleseDepartment of Medical, Oral and Biotechnological Sciences, 'G. d'Annunzio' University of Chieti-Pescara, Chieti, Italy.
University of Chieti-Pescara · ITCentre National de la Recherche Scientifique · FRInstitute of Protein Biochemistry · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane trafficking via the Golgi-localised KDEL receptor activates signalling cascades that coordinate both trafficking and other cellular functions, including autophagy and extracellular matrix degradation. In this study, we provide evidence that membrane trafficking activates KDEL receptor and the Src family kinases at focal adhesions of HeLa cells, where this phosphorylates ADP-ribosylation factor GTPase-activating protein with SH3 domain, ankyrin repeat and PH domain (ASAP)1 and focal adhesion kinase (FAK). Previous studies have reported extracellular matrix degradation at focal adhesions. Here, matrix degradation was not seen at focal adhesions, although it occurred at invadopodia, where it was increased by KDEL receptor activation. This activation of KDEL receptor at invadopodia of A375 cells promoted recruitment and phosphorylation of FAK on tyrosines 397 and 861. From the functional standpoint, FAK overexpression inhibited steady-state and KDEL-receptor-stimulated extracellular matrix degradation, whereas overexpression of the FAK-Y397F mutant only inhibited KDEL-receptor-stimulated matrix degradation. Finally, we show that the Src and FAK activated downstream of KDEL receptor are part of parallel signalling pathways. In conclusion, membrane-traffic-generated signalling via KDEL receptor activates Src not only at the Golgi complex, but also at focal adhesions. By acting on Src and FAK, KDEL receptor increases invadopodia-mediated matrix degradation.

Indexed as

cell signallingFAKKDEL receptormembrane traffickingSrc

Identifiers

PMID29535802
PMCPMC5828207
OpenAlexW2780873563

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.