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Related Concept Videos

Septins01:19

Septins

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Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...
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Role of Septins01:02

Role of Septins

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Septins are the recently discovered fourth major protein component of the cytoskeleton, along with microfilaments, microtubules, and intermediate filaments. These proteins can associate with other cytoskeletal filaments and carry out varied roles or can be free-floating in the cytoplasm.
Cellular Functions of Septins
Recent studies have revealed the multifaceted roles of septins in various cellular processes such as cytokinesis, ciliogenesis, and neurogenesis. Septins act as scaffolds and...
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The Contractile Ring02:15

The Contractile Ring

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Contractile rings are composed of microfilaments and are responsible for separating the daughter cells during cytokinesis. Contractile ring assembly proceeds along with other cell cycle events; however, very few mechanistic details are known about the timing and coordination of the contractile rings with the cell cycle.
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Cytoplasm01:24

Cytoplasm

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The cytoplasm consists of organelles and a framework of protein scaffolds called the cytoskeleton suspended in an aqueous solution, the cytosol. The cytosol is a rich broth of water, ions, salts, and various organic molecules.
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Cytoplasm01:16

Cytoplasm

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The cytoplasm consists of organelles and a framework of protein scaffolds called the cytoskeleton suspended in an aqueous solution, the cytosol. The cytosol is a rich broth of water, ions, salts, and various organic molecules.
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The Role of Actin and Myosin in Non-muscle Cells01:10

The Role of Actin and Myosin in Non-muscle Cells

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Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They  are held...
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Related Experiment Video

Updated: Dec 17, 2025

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
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Calsequestrin. Structure, function, and evolution.

Qian Wang1, Marek Michalak1

  • 1Department of Biochemistry, University of Alberta, Edmonton, AB, T6H 2S7, Canada.

Cell Calcium
|June 24, 2020
PubMed
Summary
This summary is machine-generated.

Calsequestrin, a key sarcoplasmic reticulum protein, regulates muscle calcium (Ca2+) release. Recent research highlights its structure, function, evolution, and role in muscle diseases like CPVT.

Keywords:
Calcium binding proteinCalcium storageExcitation-contraction couplingRyanodine receptorSarcoplasmic reticulumStress sensor

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Muscle Physiology

Background:

  • Calsequestrin is the primary Ca2+ binding protein in the sarcoplasmic reticulum (SR).
  • It functions in Ca2+ storage, buffering, and regulation of Ca2+ release channels in muscle.
  • Calsequestrin is crucial for excitation-contraction coupling and anchored via membrane protein interactions.

Purpose of the Study:

  • To provide a comprehensive overview of calsequestrin.
  • To discuss recent advances in its structure, function, and interactions.
  • To explore its role in muscle physiology, stress responses, and human diseases.

Main Methods:

  • Literature review of recent studies on calsequestrin.
  • Analysis of calsequestrin structure, Ca2+ binding, and polymerization.
  • Phylogenetic analysis and examination of protein-protein interactions.

Main Results:

  • Calsequestrin undergoes reversible polymerization with increasing Ca2+.
  • It communicates luminal Ca2+ changes to release channels.
  • New insights into calsequestrin trafficking, evolution, and disease links (e.g., CPVT) have emerged.

Conclusions:

  • Calsequestrin is essential for muscle Ca2+ homeostasis and excitation-contraction coupling.
  • Understanding calsequestrin is vital for insights into muscle physiology and pathology.
  • Recent research expands our knowledge of calsequestrin's diverse roles and disease relevance.