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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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Vesicular Tubular Clusters01:45

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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.
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Overview of Secretory Vesicles01:33

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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.
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SNAREs and Membrane Fusion01:43

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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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Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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Two Rab2 interactors regulate dense-core vesicle maturation.

Michael Ailion1, Mandy Hannemann2, Susan Dalton3

  • 1Howard Hughes Medical Institute, Department of Biology, University of Utah, Salt Lake City, UT 84112, USA; Department of Biochemistry, University of Washington, Seattle WA, 98195, USA.

Neuron
|April 5, 2014
PubMed
Summary
This summary is machine-generated.

Researchers identified two conserved proteins, RUND-1 and CCCP-1, crucial for dense-core vesicle maturation. These proteins, along with RAB-2, regulate the sorting of cargo within these vesicles at the trans-Golgi network.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Neuroscience

Background:

  • Peptide neuromodulators are essential signaling molecules released from dense-core vesicles.
  • Dense-core vesicle biogenesis involves cargo sorting and maturation at the trans-Golgi network.
  • Understanding the molecular machinery governing dense-core vesicle formation is critical for deciphering neuronal communication.

Purpose of the Study:

  • To identify novel proteins involved in dense-core vesicle sorting and maturation.
  • To elucidate the molecular mechanisms regulating cargo selection and trafficking within dense-core vesicles.
  • To characterize the function of conserved Rab2-binding proteins in this process.

Main Methods:

  • Genetic screening in *Caenorhabditis elegans* to identify mutants with defective dense-core vesicle function.
  • Co-localization studies to determine the subcellular localization of identified proteins.
  • Analysis of dense-core vesicle cargo sorting in wild-type and mutant strains.
  • Protein-protein interaction assays to identify binding partners.

Main Results:

  • Two conserved Rab2-binding proteins, RUND-1 (RUN domain) and CCCP-1 (coiled-coil), were identified.
  • RUND-1 and CCCP-1 colocalize with RAB-2 at the Golgi apparatus.
  • Mutants lacking rab-2, rund-1, or cccp-1 exhibit defects in sorting both soluble and transmembrane dense-core vesicle cargos.
  • RUND-1 interacts with TBC-8 (a Rab2 GAP) and RIC-19 (a RAB-2 effector).

Conclusions:

  • A conserved protein pathway involving RUND-1, CCCP-1, and RAB-2 regulates dense-core vesicle maturation.
  • These proteins play a critical role in cargo sorting at the trans-Golgi network.
  • The findings provide insights into the fundamental mechanisms of secretory vesicle biogenesis.