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Related Concept Videos

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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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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Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
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Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
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Related Experiment Video

Updated: Apr 18, 2026

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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Septin dynamics are essential for exocytosis.

Elmira Tokhtaeva1, Joe Capri2, Elizabeth A Marcus3

  • 1From the Departments of Physiology and Veterans Affairs Greater Los Angeles Healthcare System, Los Angeles, California 90073.

The Journal of Biological Chemistry
|January 11, 2015
PubMed
Summary
This summary is machine-generated.

Septin-2 proteins stimulate exocytosis by dynamically reorganizing during the process. This study reveals septin-2

Keywords:
Cell BiologyCytoskeletonExocytosisMembrane FusionMembrane TraffickingProtein SecretionSeptins

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

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Neuroscience

Background:

  • Septins are cytoskeletal proteins involved in organizing protein complexes.
  • Previous studies showed conflicting roles for septins in exocytosis.
  • The role of septin-2 in exocytosis remained unexplored.

Purpose of the Study:

  • To investigate the role of septin-2 in exocytosis.
  • To identify septin-2 interacting proteins involved in exocytosis.
  • To elucidate the mechanism of septin-2 in regulating exocytosis.

Main Methods:

  • Nano-LC-MS/MS and immunoblotting to analyze the septin-2 interactome.
  • siRNA-mediated depletion of septin-2.
  • Pharmacological inhibition of septin dynamics using forchlorfenuron.
  • Assessment of exocytosis in various cell types and primary neurons.

Main Results:

  • Septin-2 interacts with SNARE proteins, Munc-18-1, NSF, Hsc70, and synucleins.
  • Septin-2 does not interact with α-SNAP, suggesting dynamic reorganization during exocytosis.
  • Depletion or impaired dynamics of septin-2 inhibited both constitutive and stimulated exocytosis.
  • Forchlorfenuron treatment reduced SNAP-25 levels and inhibited acetylcholine secretion.

Conclusions:

  • Septin-2 plays a stimulatory role in exocytosis.
  • Dynamic reorganization of septin oligomers is crucial for exocytosis.
  • Septin-2 is a key regulator of the exocytotic machinery.