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Related Concept Videos

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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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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Nuclear Fusion02:45

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The process of converting very light nuclei into heavier nuclei is also accompanied by the conversion of mass into large amounts of energy, a process called fusion. The principal source of energy in the sun is a net fusion reaction in which four hydrogen nuclei fuse and ultimately produce one helium nucleus and two positrons.
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Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
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Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay

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PRRT2 Regulates Synaptic Fusion by Directly Modulating SNARE Complex Assembly.

Jeff Coleman1, Ouardane Jouannot1, Sathish K Ramakrishnan1

  • 1Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USA.

Cell Reports
|January 19, 2018
PubMed
Summary
This summary is machine-generated.

Mutations in proline-rich transmembrane protein 2 (PRRT2) disrupt neurotransmitter release, causing neurological disorders. This study reveals PRRT2 inhibits vesicle priming by blocking SNARE complex assembly, a function impaired by disease-associated mutations.

Keywords:
PRRT2SNARE proteinsneurotransmitter releaseparoxysmal dyskinesiasynaptic fusion

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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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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • Proline-rich transmembrane protein 2 (PRRT2) mutations link to paroxysmal neurological disorders.
  • PRRT2's role in neurotransmitter release at presynaptic terminals is established, but its mechanism remains elusive.

Purpose of the Study:

  • To elucidate the physiological function of PRRT2 in synaptic vesicle release.
  • To investigate the molecular mechanism underlying PRRT2's regulation of neurotransmitter release.
  • To correlate PRRT2 mutations with disease severity by examining their impact on function.

Main Methods:

  • Reconstituted single vesicle and bulk fusion assays.
  • Live cell imaging of single exocytotic events in PC12 cells.
  • Biophysical analysis of PRRT2 interactions.

Main Results:

  • PRRT2 selectively inhibits trans SNARE complex assembly, negatively regulating synaptic vesicle priming.
  • Weak interactions between PRRT2's N-terminal proline-rich domain and SNARE proteins mediate this inhibition.
  • Paroxysmal dyskinesia-associated PRRT2 mutations impair SNARE modulation, correlating with disease severity.

Conclusions:

  • PRRT2 acts as a negative regulator of synaptic vesicle priming through SNARE complex modulation.
  • Loss-of-function mutations in PRRT2 disrupt this regulatory mechanism, leading to paroxysmal neurological disorders.
  • Understanding PRRT2's function offers insights into the molecular basis of these neurological conditions.