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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-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,...
Histone Variants at the Centromere02:30

Histone Variants at the Centromere

Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3 variants are also...
Feedback Regulation of Calcium Concentration01:27

Feedback Regulation of Calcium Concentration

Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
Structure of Cadherins01:25

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...
Centrioles and Centrosomes01:13

Centrioles and Centrosomes

Most animal cells comprise a pair of centrioles together called a centrosome. The cell duplicates its centrosome and contains two centrosomes side-by-side, which begin to move apart during the prophase. As the centrosomes migrate to two different sides of the cell, microtubules start extending from each centrosome toward the other end. The mitotic spindle is composed of the centrosomes and their emerging microtubules.
Near the end of the prophase, also called late prophase or "prometaphase,"...
Catenins01:23

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...

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Pull-down of Calmodulin-binding Proteins
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Published on: January 23, 2012

Centrin isoforms in mammals. Relation to calmodulin.

Felix Friedberg1

  • 1Department of Biochemistry and Molecular Biology, Howard University Medical School, Washington, DC, USA. ffriedberg@howard.edu

Molecular Biology Reports
|November 8, 2006
PubMed
Summary

Calmodulin (CaM) and centrin (Cetn) are ancient calcium-binding proteins with distinct cellular roles. While CaM is ubiquitous, Cetn is localized to specific structures like cilia and centrosomes, suggesting specialized functions.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Background:

  • Calmodulin (CaM) and centrin (Cetn) are ancient calcium-binding protein families.
  • Mammals possess three identical CaM genes and four distinct Cetn genes.
  • Both protein families feature four conserved EF-hand motifs for calcium binding.

Purpose of the Study:

  • To investigate the evolutionary relationships and structural differences between CaM and Cetn subfamilies.
  • To explore the distinct cellular distribution and potential functional divergence of CaM and Cetn.

Main Methods:

  • Comparative gene analysis of CaM and Cetn in mammals and simpler eukaryotes.
  • Examination of protein structure, including unique amino acid extensions in Cetn.
  • Analysis of mRNA 3' UTRs for distinguishing gene products.
  • Review of known cellular localization and protein interaction data for CaM and Cetn.

Main Results:

  • Cetn 1 gene arose from Cetn 2 via retroposition but is expressed.
  • Cetn 2, 3, and 4 are bona fide genes.
  • Cetn proteins typically possess a protruding amino acid terminus absent in CaM.
  • Conserved EF-hand motif spacing is observed across species and subfamilies.
  • CaM is ubiquitous and interacts with numerous proteins, whereas Cetn is localized to basal bodies, cilia, and centrosomes.

Conclusions:

  • CaM and Cetn, despite structural similarities in EF-hand motifs, exhibit significant divergence in gene structure, protein extensions, and cellular functions.
  • The restricted localization of Cetn suggests specialized roles distinct from the ubiquitous functions of CaM.
  • Further research is needed to understand the selective protein interactions and functional implications of these calcium-binding protein subclasses.