Evidence map›Paper›PMID 25179631›Full record

ArticleThe Journal of cell biology2014

Cofilin recruits F-actin to SPCA1 and promotes Ca2+-mediated secretory cargo sorting.

Christine Kienzle, Nirakar Basnet, Alvaro H Crevenna, Gisela Beck, Bianca Habermann, Naoko Mizuno, Julia von Blume

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

25 citing papers in PubMed, 44 citations in OpenAlex.

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  10. Sending out molecules from the TGN.Current opinion in cell biology · 2021
    Review
  11. Review
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  15. Primary Active CaCold Spring Harbor perspectives in biology · 2020
    Review
  16. Review
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  20. Article
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 2 institutions in 1 country.

Christine KienzleMax Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Nirakar BasnetMax Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Alvaro H CrevennaPhysical Chemistry, Department of Chemistry and Biochemistry and Center for NanoScience (CeNS), Ludwig Maximilians University of Munich, 81377 Munich, Germany.
Gisela BeckMax Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Bianca HabermannMax Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Naoko MizunoMax Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Julia von BlumeMax Planck Institute of Biochemistry, 82152 Martinsried, Germany vonblume@biochem.mpg.de.
Max Planck Institute of Biochemistry · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The actin filament severing protein cofilin-1 (CFL-1) is required for actin and P-type ATPase secretory pathway calcium ATPase (SPCA)-dependent sorting of secretory proteins at the trans-Golgi network (TGN). How these proteins interact and activate the pump to facilitate cargo sorting, however, is not known. We used purified proteins to assess interaction of the cytoplasmic domains of SPCA1 with actin and CFL-1. A 132-amino acid portion of the SPCA1 phosphorylation domain (P-domain) interacted with actin in a CFL-1-dependent manner. This domain, coupled to nickel nitrilotriacetic acid (Ni-NTA) agarose beads, specifically recruited F-actin in the presence of CFL-1 and, when expressed in HeLa cells, inhibited Ca(2+) entry into the TGN and secretory cargo sorting. Mutagenesis of four amino acids in SPCA1 that represent the CFL-1 binding site also affected Ca(2+) import into the TGN and secretory cargo sorting. Altogether, our findings reveal the mechanism of CFL-1-dependent recruitment of actin to SPCA1 and the significance of this interaction for Ca(2+) influx and secretory cargo sorting.

Indexed as

Calcium SignalingActinsCalciumCalcium-Transporting ATPasesCofilin 1HeLa CellsHumansPoint MutationProtein BindingProtein Interaction Domains and MotifsProtein TransportSecretory PathwayActinsATP2C1 protein, humanCalciumCalcium-Transporting ATPasesCFL1 protein, humanCofilin 1

Identifiers

PMID25179631
PMCPMC4151145
OpenAlexW2170211418

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.