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Related Concept Videos

Role of Septins01:02

Role of Septins

1.5K
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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Structural Protein Function01:56

Structural Protein Function

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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
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Structural Protein Function01:56

Structural Protein Function

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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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ATP Synthase: Structure01:18

ATP Synthase: Structure

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ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
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The Sarcomere01:08

The Sarcomere

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A sarcomere is a microscopic segment repeating in a myofibril. The sarcomere fundamentally consists of two main myofilaments: thick filaments called myosin and thin filaments called actin. These filaments interact by sliding past each other in response to stimulus. In addition to myosin and actin, several other proteins, such as tropomyosin, troponin, titin, nebulin, myomesin, α-actinin, and dystrophin, play crucial roles in regulating, structuring, and functioning of the sarcomere.
Each...
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Related Experiment Video

Updated: May 5, 2026

Bottom-Up In Vitro Methods to Assay the Ultrastructural Organization, Membrane Reshaping, and Curvature Sensitivity Behavior of Septins
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Bottom-Up In Vitro Methods to Assay the Ultrastructural Organization, Membrane Reshaping, and Curvature Sensitivity Behavior of Septins

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Spectrin: structure, function and disease.

Rui Zhang1, ChenYu Zhang, Qi Zhao

  • 1Jiangsu Engineering Research Center for microRNA Biology and Biotechnology, State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Nanjing, 210093, China.

Science China. Life Sciences
|December 5, 2013
PubMed
Summary
This summary is machine-generated.

Spectrin, a key cytoskeletal protein, is vital for cell structure and function. Its mutations are linked to diseases like anemia and cancer, highlighting its importance in human health.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Spectrin is a large, heterodimeric cytoskeletal protein essential for cell membrane stability and cellular shape.
  • It comprises alpha and beta subunits, featuring numerous spectrin repeats.
  • Spectrin plays roles in cell adhesion, spreading, and the cell cycle.

Purpose of the Study:

  • To review recent advancements in understanding spectrin's structure and function.
  • To explore the role of spectrin in various human diseases.

Main Methods:

  • Literature review of recent scientific publications.
  • Analysis of structural and functional data of spectrin.
  • Correlation of spectrin mutations with disease phenotypes.

Main Results:

  • Spectrin's modular structure, composed of spectrin repeats, underpins its diverse functions.
  • Alterations in spectrin structure and function are implicated in diseases including hereditary hemolytic anemia, spinocerebellar ataxia type 5, and cancer.

Conclusions:

  • Spectrin is a critical protein for cellular integrity and function.
  • Understanding spectrin's structure-function relationship is crucial for developing therapies for associated diseases.