Discover Community Create You

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

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Calcium
Share to Casein Kinase II

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to HEK293 Cells

Share to Insulin-Secreting Cells

Share to Naphthyridines

Share to Phenazines

Share to Recombinant Proteins

Share to 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 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Control of TRPM3 Ion Channels by Protein Kinase CK2-Mediated Phosphorylation in Pancreatic β-Cells of the Line INS-1.PMID 34884938Read ↗

Targeting Lysosomal MCOLN1/TRPML1 Ion Channels to Finely Alleviate Diabetes Mellitus via a Ca <sup>2+</sup> - CaMKKβ-AMPK pathwaySemantic proximity Read ↗

Casein kinase-mediated phosphorylation of serine 839 is necessary for basolateral localization of the Ca²⁺-activated non-selective cation channel TRPM4.Semantic proximity Read ↗

Loss of high-frequency glucose-induced Ca2+ oscillations in pancreatic islets correlates with impaired glucose tolerance in Trpm5-/- mice.Semantic proximity Read ↗

The serine 814 of TRPC6 is phosphorylated under unstimulated conditions.Semantic proximity Read ↗

Phosphorylation states greatly regulate the activity and gating properties of Cav 3.1 T-type Ca2+ channels.Semantic proximity Read ↗

Deletion of CDKAL1 affects mitochondrial ATP generation and first-phase insulin exocytosis.Semantic proximity Read ↗

Potassium channel phosphorylation in excitable cells: providing dynamic functional variability to a diverse family of ion channels.Semantic proximity Read ↗

Protein kinase CK2 is coassembled with small conductance Ca(2+)-activated K+ channels and regulates channel gating.Semantic proximity Read ↗

Interplay of PAK1 and CAMKII in Pancreatic Beta Cell Insulin SecretionSemantic proximity Read ↗

An essential role of PI(4,5)P₂ for maintaining the activity of the transient receptor potential canonical (TRPC)4β.Semantic proximity Read ↗

Phosphorylation and degradation of tomosyn-2 de-represses insulin secretion.Semantic proximity Read ↗

A Cataract-Causing Mutation in the TRPM3 Cation Channel Disrupts Calcium Dynamics in the Lens.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.