Evidence map›Paper›PMID 7622570›Full record

ArticleThe Journal of cell biology1995

A phosphatidylinositol 4,5-bisphosphate-sensitive casein kinase I alpha associates with synaptic vesicles and phosphorylates a subset of vesicle proteins.

S D Gross, D P Hoffman, P L Fisette, P Baas, R A Anderson

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

28 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Casein kinase 1α: biological mechanisms and theranostic potential.Cell communication and signaling : CCS · 2018
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Analysis of cell type-specific expression of CK1 epsilon in various tissues of young adult BALB/c Mice and in mammary tumors of SV40 T-Ag-transgenic mice.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2010
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Regulation of Alzheimer's disease amyloid-beta formation by casein kinase I.Proceedings of the National Academy of Sciences of the United States of America · 2007
    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 1 institution in 1 country.

S D GrossDepartment of Pharmacology, University of Wisconsin Medical School, Madison 53706, USA.
D P Hoffman
P L Fisette
P Baas
R A Anderson
University of Wisconsin–Madison · US

Funding

PHOSPHOINOSITIDE SIGNALING TO AND WITHIN THE NUCLEUSR01GM051968 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ANDERSON, RICHARD A. · 1995 to 2012
$3.2M
CASEIN KINASE I REGULATION BY PI-4,5-P2R01GM038906 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI ANDERSEN, RICHARD A · 1992 to 1995
–
PHOSPHOINOSITIDE REGULATION OF ERYTHROCYTE CYTOSKELETONR29GM038906 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI ANDERSEN, RICHARD A · 1987 to 1991
–
NIGMS NIH HHS GM38906NIGMS NIH HHS GM51968
6 · The paper itself

Abstract

In interphase cells, alpha-casein kinase I (alpha-CKI) is found associated with cytosolic vesicular structures, the centrosome, and within the nucleus. To identify the specific vesicular structures with which alpha-CKI is associated, established cell lines and primary rat neurons were immunofluorescently labeled with an antibody raised to alpha-CKI. In nonneuronal cells, alpha-CKI colocalizes with vesicular structures which align with microtubules and are partially coincident with both Golgi and endoplasmic reticulum markers. In neurons, alpha-CKI colocalizes with synaptic vesicle markers. When synaptic vesicles were purified from rat brain, they were highly enriched in a CKI, based on activity and immunoreactivity. The synaptic vesicle-associated CKI is an extrinsic kinase and was eluted from synaptic vesicles and purified. This purified CKI has properties most similar to alpha-CKI. When the activities of casein kinase I or II were specifically inhibited on isolated synaptic vesicles, CKI was shown to phosphorylate a specific subset of vesicle proteins, one of which was identified as the synaptic vesicle-specific protein SV2. As with alpha-CKI, the synaptic vesicle CKI is inhibited by phosphatidylinositol 4,5-bisphosphate (PIP2). However, synthesis of PIP2 was detected only in plasma membrane-containing fractions. Therefore, PIP2 may spatially regulate CKI. Since PIP2 synthesis is required for secretion, this inhibition of CKI may be important for the regulation of secretion.

Indexed as

AnimalsBiological TransportBlotting, WesternBrainCasein KinasesCell FractionationCell MembraneCHO CellsCricetinaeFluorescent Antibody TechniqueKidneyMembrane GlycoproteinsMicroscopy, ElectronNerve Tissue ProteinsNeuronsNeurotransmitter AgentsCasein KinasesMembrane GlycoproteinsNerve Tissue ProteinsNeurotransmitter AgentsPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesProtein KinasesSv2a protein, rat

Identifiers

PMID7622570
PMCPMC2120523
OpenAlexW2141361393

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.