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Related Concept Videos

Role of Septins01:02

Role of Septins

1.7K
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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Microtubules in Signaling01:22

Microtubules in Signaling

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The primary cilium, made up of microtubules, acts as antennae on the cell surfaces for relaying external stimuli into the cells. These fine hair-like structures are present, generally one per cell. These are non-motile cilia in a 9+0 microtubules arrangement, where the central pair of microtubules are absent. The primary cilia arise from the basal body embedded in the cell membrane. Intraflagellar transport (IFT) carries requisite proteins from the cytoplasm to the cilium because the primary...
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Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

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Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
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Cytoskeletal Coordination in Cell Migration01:32

Cytoskeletal Coordination in Cell Migration

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A migrating cell changes its shape during the cyclic events of attachment and detachment from the substratum and repositions the cell organelles correspondingly. These complex events are orchestrated by the dynamic cytoskeletal network comprising actin filaments, intermediate filaments, and microtubules. Cytoskeletal crosstalk — the direct and indirect communication between the different components — is crucial for this coordination. Direct communication involves various linker...
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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: Jun 14, 2025

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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Borg3 controls septin polymerization for primary cilia formation.

Janik N Schampera1,2, Friederike Lehmann1,3,4, Ana Valeria Meléndez2,3,5

  • 1Institute for Experimental and Clinical Pharmacology and Toxicology, Faculty of Medicine, University of Freiburg, 79104 Freiburg, Germany.

Iscience
|June 12, 2025
PubMed
Summary
This summary is machine-generated.

Septins enter primary cilia as octamers and polymerize for enrichment. Borg3 (Cdc42ep5) is essential for septin filament localization and dynamics within cilia, regulated by Cdc42 activity at the ciliary base.

Keywords:
BiochemistryCell biologyOrganizational aspects of cell biology

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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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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
  • Cytoskeleton Dynamics
  • Cilia Biology

Background:

  • Septin GTPases are cytoskeletal proteins forming polymers crucial for cellular functions.
  • Septins are known to localize to primary cilia, acting as signaling hubs.
  • Their specific assembly and regulation within the confined ciliary environment remain unclear.

Purpose of the Study:

  • To investigate the oligomeric state, polymerization, and regulation of septins within primary cilia.
  • To identify factors controlling septin filament dynamics and enrichment in cilia.
  • To elucidate the role of Borg3 (Cdc42ep5) and Cdc42 in septin ciliary localization.

Main Methods:

  • Utilized cultured cells for studying septin behavior in primary cilia.
  • Employed knockout strategies for Borg3 and manipulated Cdc42 activity.
  • Observed septin localization, oligomerization, and polymerization dynamics.

Main Results:

  • Septins were found to enter cilia as octamers and require polymerization for enrichment.
  • Borg3 (Cdc42ep5) was identified as an essential component for ciliary septin filament localization.
  • Borg3 knockout or Cdc42 dysregulation impaired septin dynamics and ciliary enrichment.
  • Borg3 localization is controlled by the activity cycle of Rho-GTPase Cdc42 at the ciliary base.

Conclusions:

  • Septin octamers polymerize within cilia, a process essential for their enrichment.
  • Borg3 is a critical regulator of septin filament assembly and localization in primary cilia.
  • Cdc42 activity at the ciliary base governs Borg3 localization and, consequently, septin dynamics in cilia.