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Related Concept Videos

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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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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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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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Fusion of Secretory Vesicles with the Plasma Membrane01:26

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Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
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Intracellular Signaling Affects Focal Adhesions01:17

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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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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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SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
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Multivalent Rab interactions determine tether-mediated membrane fusion.

Anna Lürick1, Jieqiong Gao1, Anne Kuhlee2

  • 1Biochemistry Section, Department of Biology/Chemistry, University of Osnabrück, 49076 Osnabrück, Germany.

Molecular Biology of the Cell
|November 18, 2016
PubMed
Summary
This summary is machine-generated.

This study reveals that the lysosomal HOPS complex requires two Rab-binding sites for membrane fusion. Both sites on the HOPS complex are crucial for tethering and SNARE-mediated fusion at endomembranes.

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Area of Science:

  • Cell biology
  • Molecular and cell biology
  • Membrane trafficking

Background:

  • Endomembrane fusion is essential for cellular function and relies on Rab GTPases and tethering factors.
  • The function of multiple Rab-binding sites on tethering complexes is largely unexplored.

Purpose of the Study:

  • To investigate the role of the two Rab-binding sites on the lysosomal HOPS complex in Ypt7-mediated membrane fusion.
  • To determine the relative contributions of Vps39 and Vps41 in Ypt7 interaction and fusion.

Main Methods:

  • Utilized tethering and fusion assays.
  • Employed HOPS complex mutants to dissect functional roles of Rab-binding sites.
  • Investigated the impact of the Vps41 ALPS motif and its phosphorylation by Yck3.

Main Results:

  • HOPS-dependent membrane fusion requires engagement of both Ypt7-binding sites.
  • Vps39 exhibits a stronger interaction with Ypt7 compared to Vps41.
  • The Vps41 ALPS motif is dispensable for tethering and fusion but can modulate tethering upon phosphorylation.

Conclusions:

  • The lysosomal HOPS complex acts as a multivalent tethering factor.
  • Two Rab-binding sites on HOPS are critical for precise SNARE assembly and endomembrane fusion.
  • This mechanism ensures spatial regulation of fusion events at endomembranes.