Evidence map›Paper›PMID 25564607›Full record

ArticleThe Journal of biological chemistry2015

Membrane targeting of the Spir·formin actin nucleator complex requires a sequential handshake of polar interactions.

Janine Tittel, Tobias Welz, Aleksander Czogalla, Susanne Dietrich, Annette Samol-Wolf, Markos Schulte, Petra Schwille, Thomas Weidemann, Eugen Kerkhoff

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Life science alliance · 2026
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  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Spire1 and Myosin Vc promote CaCellular and molecular life sciences : CMLS · 2022
    Article
  9. Role of zinc in female reproduction.Biology of reproduction · 2021
    Review
  10. Article
  11. Article
  12. CCB is Involved in Actin-Based Axonal Transport of Selected Synaptic Proteins.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
  13. Review
  14. Review
  15. Article
  16. 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

9 authors at 3 institutions in 1 country.

Janine TittelFrom the Max Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany, Biotechnology Center (BIOTEC), Biophysics Research Group and.
Tobias WelzMolecular Cell Biology Laboratory, Department of Neurology, University Hospital Regensburg, Franz-Josef-Strauss-Allee 11, D-93053 Regensburg, Germany, and.
Aleksander CzogallaPaul Langerhans Institute, Technische Universität (TU) Dresden, Tatzberg 47-51, D-01307 Dresden, Germany, German Center for Diabetes Research (Deutsches Zentrum für Diabetesforschung), 85764 Neuherberg, Germany.
Susanne DietrichMolecular Cell Biology Laboratory, Department of Neurology, University Hospital Regensburg, Franz-Josef-Strauss-Allee 11, D-93053 Regensburg, Germany, and.
Annette Samol-WolfMolecular Cell Biology Laboratory, Department of Neurology, University Hospital Regensburg, Franz-Josef-Strauss-Allee 11, D-93053 Regensburg, Germany, and.
Markos SchulteMolecular Cell Biology Laboratory, Department of Neurology, University Hospital Regensburg, Franz-Josef-Strauss-Allee 11, D-93053 Regensburg, Germany, and.
Petra SchwilleFrom the Max Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany, Biotechnology Center (BIOTEC), Biophysics Research Group and.
Thomas WeidemannFrom the Max Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany, Biotechnology Center (BIOTEC), Biophysics Research Group and.
Eugen KerkhoffMolecular Cell Biology Laboratory, Department of Neurology, University Hospital Regensburg, Franz-Josef-Strauss-Allee 11, D-93053 Regensburg, Germany, and eugen.kerkhoff@klinik.uni-regensburg.de.
University Hospital Regensburg · DEMax Planck Institute of Biochemistry · DETechnische Universität Dresden · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Spir and formin (FMN)-type actin nucleators initiate actin polymerization at vesicular membranes necessary for long range vesicular transport processes. Here we studied in detail the membrane binding properties and protein/protein interactions that govern the assembly of the membrane-associated Spir·FMN complex. Using biomimetic membrane models we show that binding of the C-terminal Spir-2 FYVE-type zinc finger involves both the presence of negatively charged lipids and hydrophobic contributions from the turret loop that intrudes the lipid bilayer. In solution, we uncovered a yet unknown intramolecular interaction between the Spir-2 FYVE-type domain and the N-terminal kinase non-catalytic C-lobe domain (KIND) that could not be detected in the membrane-bound state. Interestingly, we found that the intramolecular Spir-2 FYVE/KIND and the trans-regulatory Fmn-2-FSI/Spir-2-KIND interactions are competitive. We therefore characterized co-expressed Spir-2 and Fmn-2 fluorescent protein fusions in living cells by fluorescence cross-correlation spectroscopy. The data corroborate a model according to which Spir-2 exists in two different states, a cytosolic monomeric conformation and a membrane-bound state in which the KIND domain is released and accessible for subsequent Fmn-2 recruitment. This sequence of interactions mechanistically couples membrane binding of Spir to the recruitment of FMN, a pivotal step for initiating actin nucleation at vesicular membranes.

Indexed as

ActinsAmino Acid SequenceForminsHEK293 CellsHumansMembrane Transport ProteinsMicrofilament ProteinsMultiprotein ComplexesNuclear ProteinsProtein Interaction MapsActinsFmn2 protein, humanForminsMembrane Transport ProteinsMicrofilament ProteinsMultiprotein ComplexesNuclear ProteinsSpir-2 protein, mouseActinForminFYVEMembrane TraffickingProtein ComplexSpirVesicles

Identifiers

PMID25564607
PMCPMC4358278
OpenAlexW2054632214

What OpenQuestion holds

Textmetadata
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.