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Related Concept Videos

Formation of Complex Ions03:45

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A type of Lewis acid-base chemistry involves the formation of a complex ion (or a coordination complex) comprising a central atom, typically a transition metal cation, surrounded by ions or molecules called ligands. These ligands can be neutral molecules like H2O or NH3, or ions such as CN− or OH−. Often, the ligands act as Lewis bases, donating a pair of electrons to the central atom. These types of Lewis acid-base reactions are examples of a broad subdiscipline called coordination...
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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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Related Experiment Video

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Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
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SNAP-25 S-Guanylation and SNARE Complex Formation.

Yusuke Kishimoto1, Takaaki Akaike2, Hideshi Ihara3

  • 1Department of Biological Science, Graduate School of Science, Osaka Prefecture University, Sakai, Japan.

Methods in Molecular Biology (Clifton, N.J.)
|October 15, 2018
PubMed
Summary

8-Nitroguanosine 3',5'-cyclic monophosphate (8-nitro-cGMP) modifies SNAP-25 protein function. This study details methods to detect 8-nitro-cGMP, S-guanylated proteins, and SNARE complexes, aiding research into exocytosis regulation.

Keywords:
8-Nitro-cGMPNitric oxideRedox signalSNAP-25SNARE complex

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Area of Science:

  • Cellular signaling
  • Neuroscience
  • Biochemistry

Background:

  • 8-Nitroguanosine 3",5"-cyclic monophosphate (8-nitro-cGMP) is a key second messenger in redox signaling.
  • Synaptosomal associated protein 25 (SNAP-25) is crucial for membrane fusion and exocytosis.
  • Previous work identified S-guanylation of SNAP-25 at cysteine 90.

Purpose of the Study:

  • To elucidate the physiological and pathophysiological significance of SNAP-25 S-guanylation.
  • To establish methods for detecting 8-nitro-cGMP and S-guanylated proteins in cells.
  • To analyze SNARE complex formation and dynamics following 8-nitro-cGMP treatment.

Main Methods:

  • Immunocytochemistry for detecting 8-nitro-cGMP and S-guanylated proteins.
  • Assays to detect SNARE complex formation in treated cells.
  • Western blotting and co-immunoprecipitation techniques.

Main Results:

  • S-guanylation of SNAP-25 enhances SNARE complex formation.
  • S-guanylation of SNAP-25 reduces SNARE complex affinity for complexin.
  • Established protocols for visualizing 8-nitro-cGMP and S-guanylated proteins.

Conclusions:

  • SNAP-25 S-guanylation modulates SNARE complex interactions, impacting exocytosis.
  • The described methods facilitate further investigation into 8-nitro-cGMP signaling pathways.
  • Understanding these modifications is vital for comprehending cellular processes and disease states.