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Related Concept Videos

Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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...
Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

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...
Cohesins02:20

Cohesins

Cohesin protein complexes are a molecular glue that holds two sister chromatids together. They play an important role both in mitosis and meiosis. In mitosis, all cohesin complexes present on the chromosomes are removed before the start of the anaphase stage.
Cohesin complexes in Meiotic Division
Meiosis involves two distinct rounds of chromosomal segregation and cell divisions— Meiosis I followed by Meiosis II – producing four daughter cells. Meiosis I includes the separation of homologous...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...

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Related Experiment Video

Updated: May 19, 2026

Protein Purification Technique that Allows Detection of Sumoylation and Ubiquitination of Budding Yeast Kinetochore Proteins Ndc10 and Ndc80
12:28

Protein Purification Technique that Allows Detection of Sumoylation and Ubiquitination of Budding Yeast Kinetochore Proteins Ndc10 and Ndc80

Published on: May 3, 2015

Seg1 controls eisosome assembly and shape.

Karen E Moreira1, Sebastian Schuck, Bianca Schrul

  • 1Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, CA 94158, USA.

The Journal of Cell Biology
|August 8, 2012
PubMed
Summary
This summary is machine-generated.

The eisosome protein Seg1 is crucial for building and shaping yeast plasma membrane structures. Seg1 acts as a scaffold, guiding the assembly of other proteins like Pil1 and Lsp1, influencing eisosome architecture.

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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
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Visualization of miniSOG Tagged DNA Repair Proteins in Combination with Electron Spectroscopic Imaging (ESI)
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Visualization of miniSOG Tagged DNA Repair Proteins in Combination with Electron Spectroscopic Imaging (ESI)

Published on: September 24, 2015

Related Experiment Videos

Last Updated: May 19, 2026

Protein Purification Technique that Allows Detection of Sumoylation and Ubiquitination of Budding Yeast Kinetochore Proteins Ndc10 and Ndc80
12:28

Protein Purification Technique that Allows Detection of Sumoylation and Ubiquitination of Budding Yeast Kinetochore Proteins Ndc10 and Ndc80

Published on: May 3, 2015

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

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Visualization of miniSOG Tagged DNA Repair Proteins in Combination with Electron Spectroscopic Imaging (ESI)
13:06

Visualization of miniSOG Tagged DNA Repair Proteins in Combination with Electron Spectroscopic Imaging (ESI)

Published on: September 24, 2015

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biophysics

Background:

  • Eisosomes are stable plasma membrane domains in Saccharomyces cerevisiae, implicated in endocytosis.
  • They are primarily composed of cytoplasmic proteins Pil1 and Lsp1, forming scaffolds around membrane invaginations.

Purpose of the Study:

  • To investigate the role of the poorly characterized protein Seg1 in eisosome biogenesis and architecture.
  • To elucidate the sequential assembly process of eisosome components.

Main Methods:

  • Genetic analysis of Seg1 function in Saccharomyces cerevisiae.
  • Microscopy techniques to visualize eisosome structure and protein localization.
  • Comparative analysis with the Seg1-like protein Sle1 in Schizosaccharomyces pombe.

Main Results:

  • Seg1 is essential for the efficient incorporation of Pil1 and the formation of normal plasma membrane furrows.
  • Seg1 acts as an early-acting platform, preceding Pil1 and Lsp1 during eisosome assembly.
  • Seg1 abundance regulates eisosome shape and length.
  • The Seg1 homolog Sle1 is necessary for filamentous eisosome formation in fission yeast.

Conclusions:

  • Seg1 plays a critical role in the stepwise biogenesis and architectural organization of eisosomes.
  • The findings reveal conserved mechanisms in yeast eisosome formation and highlight similarities with mammalian caveolae.