Evidence map›Paper›PMID 20230784›Full record

ArticleBiochemical and biophysical research communications2010

Phosphorylation by Nek1 regulates opening and closing of voltage dependent anion channel 1.

Yumay Chen, Maria Gaczynska, Pawel Osmulski, Rosaria Polci, Daniel J Riley

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

31 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  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

5 authors at 3 institutions in 1 country.

Yumay ChenDepartment of Medicine, Division of Endocrinology, University of California, Irvine, USA. yumayc@uci.edu
Maria Gaczynska
Pawel Osmulski
Rosaria Polci
Daniel J Riley
Biotechnology Institute · USThe University of Texas Health Science Center at San Antonio · USUniversity of California, Irvine · US

Funding

Transgenic Animal and Morphology CoreP50DK061597 · NIDDK · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI HASTY, EDWARD PAUL · 2003 to 2007
$5.0M
Pathogenic Mechanism of Polycystic Kidney DiseaseR01DK067339 · NIDDK · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI CHEN, YUMAY · 2006 to 2010
$1.2M
Cell Cycle Dependent Mechanisms of Renal HypertrophyR01DK061626 · NIDDK · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI RILEY, DANIEL J · 2002 to 2006
$1.0M
NIDDK NIH HHS P50 DK061597NIDDK NIH HHS P50-DK061597NIDDK NIH HHS R01 DK061626NIDDK NIH HHS R01 DK067339NIDDK NIH HHS R01-DK067339NIDDK NIH HHS R01-DK61626
6 · The paper itself

Abstract

VDAC1 is a key component of the mitochondrial permeability transition pore. To initiate apoptosis and certain other forms of cell death, mitochondria become permeable such that cytochrome c and other pre-apoptotic molecules resident inside the mitochondria enter the cytosol and activate apoptotic cascades. We have shown recently that VDAC1 interacts directly with never-in-mitosis A related kinase 1 (Nek1), and that Nek1 phosphorylates VDAC1 on Ser193 to prevent excessive cell death after injury. How this phosphorylation regulates the activity of VDAC1, however, has not yet been reported. Here, we use atomic force microscopy (AFM) and cytochrome c conductance studies to examine the configuration of VDAC1 before and after phosphorylation by Nek1. Wild-type VDAC1 assumes an open configuration, but closes and prevents cytochrome c efflux when phosphorylated by Nek1. A VDAC1-Ser193Ala mutant, which cannot be phosphorylated by Nek1 under identical conditions, remains open and constitutively allows cytochrome c efflux. Conversely, a VDAC1-Ser193Glu mutant, which mimics constitutive phosphorylation by Nek1, remains closed by AFM and prevents cytochrome c leakage in the same liposome assays. Our data provide a mechanism to explain how Nek1 regulates cell death by affecting the opening and closing of VDAC1.

Indexed as

Cell Cycle ProteinsCell LineCytochromesErythrocyte MembraneHumansLiposomesMicroscopy, Atomic ForceMutationNIMA-Related Kinase 1PhosphorylationProtein Serine-Threonine KinasesRecombinant ProteinsSerineVoltage-Dependent Anion Channel 1Cell Cycle ProteinsCytochromesLiposomesNEK1 protein, humanNIMA-Related Kinase 1Protein Serine-Threonine KinasesRecombinant ProteinsSerineVDAC1 protein, humanVoltage-Dependent Anion Channel 1

Identifiers

PMID20230784
PMCPMC2859727
OpenAlexW2003249572

What OpenQuestion holds

Textmetadata
LicenceTDM
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.