Control of TRPM3 Ion Channels by Protein Kinase CK2-Mediated Phosphorylation in Pancreatic β-Cells of the Line INS-1.

doi:10.3390/ijms222313133

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

Control of TRPM3 Ion Channels by Protein Kinase CK2-Mediated Phosphorylation in Pancreatic β-Cells of the Line INS-1.

International journal of molecular sciences - 4 Dec 2021

Becker Alexander, Götz Claudia, Montenarh Mathias, Philipp Stephan E

Abstract excerpt

In pancreatic β-cells of the line INS-1, glucose uptake and metabolism induce the openings of Ca2+-permeable TRPM3 channels that contribute to the elevation of the intracellular Ca2+ concentration and the fusion of insulin granules with the plasma membrane. Conversely, glucose-induced Ca2+ signals and insulin release are reduced by the activity of the serine/threonine kinase CK2. Therefore, we hypothesized that...

Topics

Animals
Calcium
Casein Kinase II
Cell Line
HEK293 Cells
Humans
Insulin-Secreting Cells
Mutation
Naphthyridines
Phenazines
Phosphorylation
Pregnenolone
Rats
Recombinant Proteins
TRPM Cation Channels

Source

Open in PubMed Open full text

Identifiers

PMID: 34884938
DOI: 10.3390/ijms222313133
PMCID: PMC8658122

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics