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Related Concept Videos

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...
Lysosomes01:31

Lysosomes

Lysosomes are membrane-enclosed spherical sacs derived from the Golgi apparatus. The most important function of the lysosome is degrading macromolecules and biological polymers that are released during membrane trafficking events such as the secretory, endocytic, autophagic, and phagocytic pathways. The degradation is carried out by several hydrolytic enzymes active in an acidic environment of the lysosomal lumen. These acid hydrolases are involved in cellular processes such as cell signaling,...
Yeast Signaling01:28

Yeast Signaling

Yeasts are single-celled organisms, but unlike bacteria, they are eukaryotes (cells with a nucleus). Cell signaling in yeast is similar to signaling in other eukaryotic cells. A ligand, such as a protein or a small molecule released from a yeast cell, attaches to a receptor on the cell surface. The binding stimulates second-messenger kinases to activate or inactivate transcription factors that further regulate gene expression. Many of the yeast intracellular signaling cascades have similar...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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 translocon complex.
Membrane Proteins01:30

Membrane Proteins

Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...
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Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...

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Related Experiment Video

Updated: Jun 28, 2026

Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae
08:55

Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae

Published on: July 19, 2021

The yeast vacuolar membrane proteome.

Elena Wiederhold1, Tejas Gandhi, Hjalmar P Permentier

  • 1Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute and Zernike Institute for Advanced Materials, University of Groningen, Groningen, The Netherlands.

Molecular & Cellular Proteomics : MCP
|November 13, 2008
PubMed
Summary

Researchers identified 148 proteins in yeast vacuole membranes, revealing novel transporters for nucleosides and oligopeptides. This study enhances understanding of vacuolar transport and protein localization in cellular functions.

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Measurement of Vacuolar and Cytosolic pH In Vivo in Yeast Cell Suspensions
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Measurement of Vacuolar and Cytosolic pH In Vivo in Yeast Cell Suspensions

Published on: April 19, 2013

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Last Updated: Jun 28, 2026

Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae
08:55

Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae

Published on: July 19, 2021

Measurement of Vacuolar and Cytosolic pH In Vivo in Yeast Cell Suspensions
13:55

Measurement of Vacuolar and Cytosolic pH In Vivo in Yeast Cell Suspensions

Published on: April 19, 2013

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Vacuoles are essential organelles with critical roles in ion homeostasis, detoxification, storage, and proteolysis.
  • Solute transport across the vacuolar membrane is vital for these functions.
  • Identifying vacuolar membrane proteins is key to understanding vacuolar transport mechanisms.

Purpose of the Study:

  • To identify proteins responsible for solute transport across the vacuolar membrane in Saccharomyces cerevisiae.
  • To characterize the vacuolar membrane proteome and discover novel transporters.

Main Methods:

  • Purification of Saccharomyces cerevisiae vacuoles.
  • Subtractive proteomics to differentiate true vacuolar proteins from contaminants.
  • Statistical analysis including enrichment ranking and iterative group analysis.

Main Results:

  • 148 proteins were significantly enriched in pure vacuolar preparations.
  • Identified known vacuolar proteins (e.g., V-ATPase subunits) and novel proteins, including potential nucleoside and oligopeptide transporters.
  • Observed enrichment of proteins involved in membrane fusion and trafficking, suggesting broader roles or multiple localizations.

Conclusions:

  • The study provides a comprehensive dataset of vacuolar membrane proteins.
  • Identified novel candidates for vacuolar solute transporters, advancing the understanding of vacuolar function.
  • Highlights the complexity of protein localization and potential inaccuracies in current cellular annotations.