Structural highlights
Function
CALM1_RAT Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2.[UniProtKB:P62158]MYLK_CHICK Phosphorylates a specific serine in the N-terminus of a myosin light chain, which leads to the formation of calmodulin/MLCK signal transduction complexes which allow selective transduction of calcium signals.GFP_AEQVI Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
Publication Abstract from PubMed
Self-complementing bipartite fluorescent proteins (FPs) are useful tools for the detection of protein-protein proximity and for localizing fluorophores to membrane-membrane contact sites. Here, we report versions of circularly permuted green FP (GFP), red FP (RFP), and mNeonGreen (NG), which are split into a large fragment composed of nine beta-strands and a small fragment composed of two beta-strands. In each case, the large and small fragments can associate in live cells to form the complete 11-stranded FP beta-barrel. We further converted each of these three self-complementing FPs into bipartite calcium ion (Ca(2+)) biosensors. We demonstrate that appropriately targeted versions of these split FPs, and split FP-based biosensors, can be functionally assembled at membrane-membrane contact sites. We employ the bipartite NG-based Ca(2+) biosensor for visualization of pharmacologically induced Ca(2+) release at mitochondria-endoplasmic reticulum contact sites (MERCs).
Bipartite Genetically Encoded Biosensors to Sense Calcium Ion Dynamics at Membrane-Membrane Contact Sites.,Yamaguchi I, Barazzuol L, Dematteis G, Zhu W, Wen Y, Drobizhev M, Lim D, Campbell RE, Cali T, Nasu Y Anal Chem. 2025 Sep 16;97(36):19848-19861. doi: 10.1021/acs.analchem.5c03831. , Epub 2025 Sep 1. PMID:40888292[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yamaguchi I, Barazzuol L, Dematteis G, Zhu W, Wen Y, Drobizhev M, Lim D, Campbell RE, Calì T, Nasu Y. Bipartite Genetically Encoded Biosensors to Sense Calcium Ion Dynamics at Membrane-Membrane Contact Sites. Anal Chem. 2025 Sep 16;97(36):19848-19861. PMID:40888292 doi:10.1021/acs.analchem.5c03831
