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Related Concept Videos

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As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.
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Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
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While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
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Rational functions are expressions written as the ratio of two polynomials, and their integrals are evaluated by simplifying the integrand into manageable parts. These functions are classified as proper or improper based on the degrees of the numerator and denominator.A rational function is proper when the degree of the numerator is less than the degree of the denominator. In this case, partial fraction decomposition is used to rewrite the function as a sum of simpler rational terms. The...
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The Earth and its atmosphere have provided humans with air, water, and food, but these are not the only requirements for survival. Humans also require a specific range of temperature and pressure that the Earth and its atmosphere provides.
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Related Experiment Video

Updated: Jan 30, 2026

Fabrication of a Bioactive, PCL-based "Self-fitting" Shape Memory Polymer Scaffold
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A SEPT1-based scaffold is required for Golgi integrity and function.

Kyungyeun Song1, Claudia Gras1, Gabrielle Capin1

  • 1Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP) Berlin, Molecular Pharmacology and Cell Biology, 13125 Berlin, Germany.

Journal of Cell Science
|February 3, 2019
PubMed
Summary
This summary is machine-generated.

Septin 1 (SEPT1) forms a scaffold at the Golgi, crucial for its structure and function by organizing microtubules. SEPT1 depletion causes Golgi fragmentation and disrupts membrane traffic.

Keywords:
CEP170GM130GolgiMicrotubule nucleationSEPT1Septin

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cytoskeleton Dynamics

Background:

  • Septin GTPases are known for scaffolding at the plasma membrane.
  • Their roles at intracellular membranes, particularly the Golgi apparatus, are largely unknown.
  • Understanding organelle compartmentalization is key to eukaryotic cell function.

Purpose of the Study:

  • To investigate the role of septins at intracellular membranes.
  • To determine the function of septin 1 (SEPT1) in Golgi apparatus structure and dynamics.
  • To elucidate the molecular mechanisms underlying Golgi organization by SEPT1.

Main Methods:

  • Immunofluorescence microscopy to visualize Golgi structure and SEPT1 localization.
  • Depletion studies using siRNA to assess the impact of SEPT1 loss.
  • Co-immunoprecipitation assays to identify interacting proteins.
  • Microtubule nucleation assays.

Main Results:

  • SEPT1 localizes to the Golgi and forms a scaffold essential for its structural integrity.
  • SEPT1 promotes local microtubule nucleation and Golgi positioning via interaction with GM130 and centrosomal proteins (CEP170, γ-Turc).
  • SEPT1 depletion leads to Golgi ribbon fragmentation and impaired anterograde membrane transport.

Conclusions:

  • Septin 1 is a critical regulator of Golgi organization and function.
  • SEPT1 acts as a scaffold linking the Golgi to the microtubule cytoskeleton.
  • Disruption of SEPT1 function severely impacts Golgi morphology and membrane trafficking.