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Related Concept Videos

Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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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...
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Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
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Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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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...
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Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

3.3K
After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
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Protein Transport to the Thylakoids01:22

Protein Transport to the Thylakoids

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Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
3.1K
Rab Cascades01:25

Rab Cascades

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Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
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Related Experiment Video

Updated: Mar 21, 2026

Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein
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Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein

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TBC1D14 sets the TRAPP for ATG9.

Christopher A Lamb1, Sharon A Tooze1

  • 1a The Francis Crick Institute, Molecular Cell Biology of Autophagy, Lincoln's Inn Fields Laboratories , London , UK.

Autophagy
|May 13, 2016
PubMed
Summary

Amino acid withdrawal triggers autophagy, forming double-membrane vesicles called autophagosomes. This process relies on membrane supply and regulated vesicle trafficking pathways involving various organelles and proteins.

Area of Science:

  • Cellular biology
  • Molecular biology
  • Autophagy research

Background:

  • Autophagy is a cellular process involving the formation of double-membrane vesicles (autophagosomes) to degrade cellular components.
  • Amino acid withdrawal is a known inducer of autophagy.
  • Autophagosome formation requires a significant membrane supply and intricate molecular regulation of vesicle trafficking.

Purpose of the Study:

  • To investigate the membrane sources and regulatory mechanisms involved in autophagosome formation during starvation.
  • To understand the role of various organelles and membrane traffic regulators in initiating and forming autophagosomes.

Main Methods:

  • The study focuses on identifying membrane sources contributing to autophagosome formation.
  • It examines the involvement of key regulators in membrane trafficking, such as RAB proteins, SNARE proteins, and BAR domain-containing proteins.
Keywords:
ATG9RAB proteinTBC1D14TRAPPautophagyendosomegolgi

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Tandem Affinity Purification of Protein Complexes from Eukaryotic Cells
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Main Results:

  • Amino acid withdrawal rapidly induces autophagosome formation within 10-15 minutes.
  • Multiple membrane sources, including the ER, Golgi, plasma membrane, mitochondria, and recycling endosomes, contribute to autophagosome biogenesis.
  • Proteins involved in membrane trafficking, including small GTPases (RAB proteins), SNAREs, and BAR domain proteins, play crucial roles in supporting autophagosome formation.

Conclusions:

  • Autophagosome formation is a complex process requiring coordinated membrane supply and vesicle trafficking.
  • The identified membrane sources and regulatory proteins are critical for efficient autophagy initiation and completion.
  • Further research into these regulatory mechanisms can provide insights into cellular stress responses and disease.