Evidence map›Paper›PMID 19460754›Full record

ArticleThe Journal of biological chemistry2009

CAPS activity in priming vesicle exocytosis requires CK2 phosphorylation.

Mari Nojiri, Kelly M Loyet, Vadim A Klenchin, Gregory Kabachinski, Thomas F J Martin

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

11 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. CK2 Phosphorylation Is Required for Regulation of Syntaxin 1A Activity in CaInternational journal of molecular sciences · 2021
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. CAPS and Munc13: CATCHRs that SNARE Vesicles.Frontiers in endocrinology · 2013
    Review
  9. Article
  10. Article
  11. 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 1 institution in 1 country.

Mari NojiriDepartment of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
Kelly M Loyet
Vadim A Klenchin
Gregory Kabachinski
Thomas F J Martin
University of Wisconsin–Madison · US

Funding

THE MECHANISM OF ACTION OF THYROTROPIN-RELEASING HORMONER01DK025861 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI MARTIN, THOMAS F. J. · 1986 to 2024
$5.6M
CA++ REGULATION OF SECRETION IN NEUROENDOCRINE CELLSR01DK040428 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI MARTIN, THOMAS F. J. · 1988 to 2015
$4.8M
THE MECHANISM OF ACTION OF THYROTROPIN-RELEASING HORMONER37DK025861 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI MARTIN, THOMAS F. J. · 1991 to 2008
$3.3M
NIDDK NIH HHS DK25861NIDDK NIH HHS DK40428NIDDK NIH HHS R01 DK025861NIDDK NIH HHS R01 DK040428NIDDK NIH HHS R37 DK025861
6 · The paper itself

Abstract

CAPS (Ca(2+)-dependent activator protein for secretion) functions in priming Ca(2+)-dependent vesicle exocytosis, but the regulation of CAPS activity has not been characterized. Here we show that phosphorylation by protein kinase CK2 is required for CAPS activity. Dephosphorylation eliminated CAPS activity in reconstituting Ca(2+)-dependent vesicle exocytosis in permeable and intact PC12 cells. Ser-5, -6, and -7 and Ser-1281 were identified by mass spectrometry as the major phosphorylation sites in the 1289 residue protein. Ser-5, -6, and -7 but not Ser-1281 to Ala substitutions abolished CAPS activity. Protein kinase CK2 phosphorylated CAPS in vitro at these sites and restored the activity of dephosphorylated CAPS. CK2 is the likely in vivo CAPS protein kinase based on inhibition of phosphorylation by tetrabromo-2-benzotriazole in PC12 cells and by the identity of in vivo and in vitro phosphorylation sites. CAPS phosphorylation by CK2 was constitutive, but the elevation of Ca(2+) in synaptosomes increased CAPS Ser-5 and -6 dephosphorylation, which terminates CAPS activity. These results identify a functionally important N-terminal phosphorylation site that regulates CAPS activity in priming vesicle exocytosis.

Indexed as

ExocytosisAmino Acid SequenceAnimalsCalciumCalcium-Binding ProteinsCasein Kinase IIChlorocebus aethiopsCOS CellsHumansMiceMolecular Sequence DataPC12 CellsPhosphorylationRatsSequence Homology, Amino AcidSerinebenzotriazoleCadps protein, ratCalciumCalcium-Binding ProteinsCasein Kinase IISerineTriazoles

Identifiers

PMID19460754
PMCPMC2707249
OpenAlexW1990113281

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.