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Related Concept Videos

Polarity of the Cytoskeleton01:18

Polarity of the Cytoskeleton

The intrinsic polarity of cells can be primarily attributed to two factors- i) the asymmetric accumulation of mobile components such are regulatory molecules and subcellular components across the cell and ii) the orientation of polar cytoskeletal filaments that make up the cytoskeletal networks, specifically microfilaments, and microtubules arranged along the axis of polarity. Interactions between the cytoskeletal filaments are crucial for the establishment and maintenance of the polar nature...
Septins01:19

Septins

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...
Studying the Cytoskeleton01:17

Studying the Cytoskeleton

The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
Adaptability of Cytoskeletal Filaments01:12

Adaptability of Cytoskeletal Filaments

The cytoskeleton is a complex dynamic structure performing varied functions based on cellular requirements. The adaptability of the individual filaments in the cytoskeleton determines their ability to perform various functions within the cell. It can undergo rapid reorganization during processes like cell division or remain stable for several hours as in the interphase. The adaptability of these filaments depends on stringent regulatory mechanisms. The microfilament and microtubules of the...
Role of Septins01:02

Role of Septins

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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Related Experiment Video

Updated: Jul 19, 2026

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions
06:32

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions

Published on: July 28, 2022

Spectrin organization and dynamics: new insights.

Abhijit Chakrabarti1, Devaki A Kelkar, Amitabha Chattopadhyay

  • 1Biophysics Division, Saha Institute of Nuclear Physics, Kolkata 700 064, India. abhijit.chakrabarti@saha.ac.in

Bioscience Reports
|October 10, 2006
PubMed
Summary

Spectrin, a key erythrocyte cytoskeleton protein, binds hydrophobic ligands and interacts with membranes. Its unique structure and chaperone activity are crucial for cellular functions in health and disease.

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Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
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Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

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Last Updated: Jul 19, 2026

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions
06:32

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions

Published on: July 28, 2022

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

Published on: August 17, 2022

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Spectrin is the primary protein in the erythrocyte cytoskeleton.
  • It forms a filamentous network supporting membrane proteins.

Purpose of the Study:

  • To review spectrin organization, focusing on hydrophobic ligand binding and membrane interactions.
  • To discuss the role of tryptophan residues in spectrin's function.
  • To highlight spectrin's chaperone-like activity.

Main Methods:

  • Review of existing literature on spectrin organization.
  • Analysis of fluorescent hydrophobic probe (Prodan, pyrene) binding to spectrin.
  • Discussion of spectrin's structural integrity post-denaturation.

Main Results:

  • Spectrin exhibits characteristic binding of hydrophobic probes, indicating specific binding site polarity.
  • Conserved tryptophan residues within 'spectrin repeats' contribute to these interactions.
  • Spectrin demonstrates chaperone-like activity and retains structural integrity after denaturation.

Conclusions:

  • Spectrin's hydrophobic binding sites and structural properties are key to its function.
  • Further research is needed to elucidate spectrin's role in cellular physiology and disease states.