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Related Concept Videos

Septins01:19

Septins

1.6K
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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Structure of Porins01:21

Structure of Porins

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Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
3.0K
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

10.4K
Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
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Protein Complex Assembly02:41

Protein Complex Assembly

12.5K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
12.5K
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

2.0K
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
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Related Experiment Video

Updated: May 3, 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

2.0K

Septin assemblies form by diffusion-driven annealing on membranes.

Andrew A Bridges1, Huaiying Zhang, Shalin B Mehta

  • 1Department of Biological Sciences, Dartmouth College, Hanover, NH 03755.

Proceedings of the National Academy of Sciences of the United States of America
|January 29, 2014
PubMed
Summary
This summary is machine-generated.

Septins, crucial for cell structure, assemble into filaments via a membrane-dependent process called annealing. This mechanism allows cells to build large septin structures from small cytosolic complexes.

Keywords:
biophysicscytoskeleton

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Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
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Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution

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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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Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions
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Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
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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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Bottom-Up In Vitro Methods to Assay the Ultrastructural Organization, Membrane Reshaping, and Curvature Sensitivity Behavior of Septins

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Biophysics

Background:

  • Septins are essential cytoskeletal proteins forming filaments and higher-order structures.
  • Their roles in cell division, polarity, and membrane remodeling are established.
  • Mechanisms of septin filament elongation and assembly remain poorly understood.

Purpose of the Study:

  • To investigate the in vivo and in vitro mechanisms of septin filament elongation and assembly.
  • To identify the role of membranes in septin higher-order structure formation.
  • To characterize the dynamics and properties of septin assemblies.

Main Methods:

  • Fluorescence correlation spectroscopy (FCS) to analyze cytosolic septin complex size.
  • Total internal reflection fluorescence microscopy (TIRFm) to observe septin dynamics on the plasma membrane.
  • In vitro reconstitution assays using purified septins and supported lipid bilayers.

Main Results:

  • Cytosolic septins exist as small complexes, not pre-formed filaments.
  • Septin complexes diffuse in 2D on the plasma membrane and assemble via end-on associations (annealing).
  • In vitro reconstitution confirmed annealing as a membrane-dependent process; filaments are flexible and grow only at ends.

Conclusions:

  • Annealing is a novel, intrinsic mechanism for septin assembly, driven by membrane interactions.
  • Cells utilize annealing to construct large, functional septin scaffolds.
  • This study reveals fundamental principles of cytoskeletal filament formation.