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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

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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
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Tail-anchoring of Proteins in the ER Membrane01:45

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Overview of Secretory Vesicles01:33

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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.
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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.
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Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
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Related Experiment Video

Updated: Apr 19, 2026

Author Spotlight: Optimizing Dendritic Spine Analysis for Balanced Manual and Automated Assessment in the Hippocampus CA1 Apical Dendrites
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A Septin-Dependent Diffusion Barrier at Dendritic Spine Necks.

Helge Ewers1, Tomoko Tada2, Jennifer D Petersen1

  • 1Université de Bordeaux, Interdisciplinary Institute for Neuroscience, UMR 5297, F-33000 Bordeaux, France; CNRS, Interdisciplinary Institute for Neuroscience, UMR 5297, F-33000 Bordeaux, France.

Plos One
|December 11, 2014
PubMed
Summary
This summary is machine-generated.

Septin7 (Sept7) forms a barrier at dendritic spine necks, regulating membrane protein diffusion. Suppressing Sept7 increases membrane molecule exploration, indicating its role in controlling spine access.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Excitatory glutamatergic synapses at dendritic spines modulate receptor content via lateral membrane diffusion.
  • Spine neck geometry is known to impede molecular access to the spine head, but the existence of a physical barrier remains unclear.

Purpose of the Study:

  • To investigate if the septin cytoskeletal GTPase complex at the spine neck regulates diffusion across it.
  • To determine the role of Septin7 (Sept7) in controlling membrane protein access to dendritic spines.

Main Methods:

  • Localization of Septin7 (Sept7) at the spine neck during development.
  • Measurement of diffusion rates for receptors, bulk membrane, and cytoplasmic proteins in spines with and without Sept7.
  • RNA interference to suppress Sept7 expression and observe effects on membrane molecule diffusion.

Main Results:

  • Septin7 (Sept7) forms a stable structure at the base of the spine neck.
  • Diffusion of receptors and bulk membrane molecules is significantly slower in spines with Sept7.
  • Suppression of Sept7 leads to increased exploration of membrane areas by membrane molecules.

Conclusions:

  • Septin7 (Sept7) acts as a regulator of diffusion across the dendritic spine neck.
  • The septin complex at the spine neck presents a physical barrier that modulates membrane protein access to spines.