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Related Concept Videos

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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Rab Proteins01:14

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
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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
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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.
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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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SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

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Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
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Author Spotlight: Image-Based Methods to Study Membrane Trafficking Events in Stomatal Lineage Cells
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TRAPP complexes in membrane traffic: convergence through a common Rab.

Jemima Barrowman1, Deepali Bhandari, Karin Reinisch

  • 1Department of Cell Biology, The Johns Hopkins School of Medicine, Baltimore, Maryland 21205, USA.

Nature Reviews. Molecular Cell Biology
|October 23, 2010
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Summary
This summary is machine-generated.

Transport protein particle (TRAPP) complexes regulate membrane trafficking. Three TRAPP forms activate specific GTPases and tether vesicles for ER-Golgi, intra-Golgi, or autophagy pathways.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Transport protein particle (TRAPP) is a guanine nucleotide-exchange factor crucial for membrane trafficking.
  • TRAPP acts on yeast Ypt1 GTPase and its mammalian homologue, RAB1.
  • TRAPP complexes are implicated in diverse cellular processes.

Purpose of the Study:

  • To elucidate the distinct roles of different TRAPP complex forms in membrane trafficking.
  • To understand how TRAPP complexes link GTPase activation to specific tethering events.

Main Methods:

  • The study likely involved biochemical assays to characterize TRAPP complex function.
  • Genetic approaches in yeast and mammalian cell models may have been used.
  • Analysis of protein interactions and localization was probably performed.

Main Results:

  • TRAPP complexes share a common core but have distinct subunits that regulate localization.
  • TRAPPI and TRAPPII are involved in endoplasmic reticulum to Golgi and intra-Golgi transport, respectively.
  • TRAPPIII has been identified as essential for autophagy.

Conclusions:

  • TRAPP complexes exhibit functional specialization based on their distinct subunits.
  • TRAPP's role in membrane trafficking is diverse, coordinating Ypt1/RAB1 activation with specific tethering events.
  • These findings provide a framework for understanding TRAPP-mediated regulation of vesicle transport and autophagy.