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Related Concept Videos

Endoplasmic Reticulum01:39

Endoplasmic Reticulum

Endoplasmic ReticulumThe endoplasmic reticulum (ER) is an extensive network of membranous sacs and tubules in eukaryotic cells, continuous with the outer membrane of the nucleus. This structural continuity integrates nuclear and cytoplasmic processes and facilitates efficient intracellular transport. This allows mRNA to move directly from the nucleus to ribosomes for efficient protein synthesis. As a result, the ER serves as a central site for the synthesis, processing, and distribution of...
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...
Golgi Apparatus01:49

Golgi Apparatus

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.The Golgi apparatus is a major sorting and dispatch station for the products of the ER. Newly arriving vesicles enter...
Golgi Apparatus01:09

Golgi Apparatus

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.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
Golgi Apparatus01:09

Golgi Apparatus

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.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
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.

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Related Experiment Video

Updated: Jun 15, 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

Requirements for transitional endoplasmic reticulum site structure and function in Saccharomyces cerevisiae.

Polina Shindiapina1, Charles Barlowe

  • 1Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.

Molecular Biology of the Cell
|March 5, 2010
PubMed
Summary

Transitional ER (tER) sites in yeast are stable structures essential for protein export. Their assembly and maintenance depend on fatty acid synthesis and specific proteins, not just COPII budding.

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Applications of pHluorin for Quantitative, Kinetic and High-throughput Analysis of Endocytosis in Budding Yeast
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Applications of pHluorin for Quantitative, Kinetic and High-throughput Analysis of Endocytosis in Budding Yeast

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Last Updated: Jun 15, 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

Applications of pHluorin for Quantitative, Kinetic and High-throughput Analysis of Endocytosis in Budding Yeast
10:02

Applications of pHluorin for Quantitative, Kinetic and High-throughput Analysis of Endocytosis in Budding Yeast

Published on: October 23, 2016

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Secretory proteins are exported from the endoplasmic reticulum (ER) via specialized transitional ER (tER) sites.
  • Coat protein complex II (COPII) proteins are crucial for ER export but the assembly and maintenance mechanisms of tER sites remain unclear.

Purpose of the Study:

  • To investigate the dynamic properties of tER sites in Saccharomyces cerevisiae.
  • To identify protein and lipid requirements for tER site structure and function.

Main Methods:

  • Utilized thermosensitive sec12 and sec16 mutations to study tER site collapse.
  • Assessed the impact of inhibiting fatty acid, sterol, and ceramide synthesis on tER sites.
  • Developed an in vitro assay to monitor Sec23p-GFP assembly at tER sites and tested lipid requirements.

Main Results:

  • tER site collapse was observed in sec12 and sec16 mutants, dependent on secretory cargo.
  • Fatty acid synthesis was essential for ER export and tER site structure; sterol and ceramide synthesis had minor effects.
  • In vitro assays showed tER sites are stable for ~10 min, depend on Sec12p, and require bulk phospholipids, but not specifically phosphatidylinositol for structure.

Conclusions:

  • tER sites are stable structures maintained by specific protein and lipid components.
  • Fatty acid synthesis is critical for tER site integrity and function.
  • tER site stability is independent of COPII budding under certain conditions, suggesting a robust underlying scaffold.