Related Experiment Video
Updated: May 15, 2026
07:51
Pull-down of Calmodulin-binding Proteins
Published on: January 23, 2012
Human calmodulin methyltransferase: expression, activity on calmodulin, and Hsp90 dependence
Sophia Magen1, Roberta Magnani, Sitvanit Haziza
1Shraga Segal Department of Microbiology, Virology and Genetics, Faculty of Health Sciences, Ben Gurion University of the Negev, Beer Sheva, Israel.
Plos One
|January 4, 2013
Summary
Calmodulin-lysine N-methyltransferase (CaM KMT) is essential for calmodulin methylation in human cells. Loss of CaM KMT causes hypomethylated calmodulin accumulation, indicating no compensatory methylation mechanisms exist.
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- Calmodulin-lysine N-methyltransferase (CaM KMT), previously C2orf34, plays a role in two multigene deletion syndromes.
- Previous studies on CaM KMT are limited, necessitating further investigation into its function and expression.
Purpose of the Study:
- To investigate the role of CaM KMT in calmodulin methylation.
- To characterize CaM KMT expression at transcript and protein levels.
- To identify CaM KMT interactions and cellular localization.
Main Methods:
- Analysis of cells from 2p21 deletion patients.
- Transcript and protein expression studies (Western blot, immunofluorescence).
- Interaction studies with Hsp90 and geldanamycin treatment.
Main Results:
- Loss of CaM KMT in 2p21 deletion patients leads to hypomethylated calmodulin accumulation.
- Identified novel CaM KMT transcripts originating from alternative exons.
- CaM KMT localizes to cytoplasm and nucleus; a short isoform is in the Golgi.
- CaM KMT broadly expressed in mouse tissues and interacts with Hsp90.
Conclusions:
- CaM KMT is the primary methyltransferase for calmodulin in human cells.
- CaM KMT is a novel Hsp90 client protein.
- Findings provide insights into CaM KMT's contribution to deletion syndrome phenotypes.
Related Concept Videos
01:16Calmodulin-dependent Signaling
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
01:58Cell Specific Gene Expression
Multicellular organisms contain a variety of structurally and functionally distinct cell types, but the DNA in all the cells originated from the same parent cells. The differences in the cells can be attributed to the differential gene expression. Liver cells, whose functions include detoxification of blood, production of bile to metabolize fats, and synthesis of proteins essential for metabolism, must express a specific set of genes to perform their functions. Gene expression also varies with...