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Phylogenetic Analysis of the In Vitro Protein-Protein Interactions Between the PDZ Domain of Rab3-Interacting Molecule (RIM), and the Extreme C-Terminus (CT) of Voltage-Gated Calcium (CaV2) Channels
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Phylogenetic Analysis of the In Vitro Protein-Protein Interactions Between the PDZ Domain of Rab3-Interacting Molecule (RIM), and the Extreme C-Terminus (CT) of Voltage-Gated Calcium (CaV2) Channels
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Phylogenetic Analysis of the In Vitro Protein-Protein Interactions Between the PDZ Domain of Rab3-Interacting Molecule (RIM), and the Extreme C-Terminus (CT) of Voltage-Gated Calcium (CaV2) Channels
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Dissertation
Phylogenetic Analysis of the In Vitro Protein-Protein Interactions Between the PDZ Domain of Rab3-Interacting Molecule (RIM), and the Extreme C-Terminus (CT) of Voltage-Gated Calcium (CaV2) Channels
2023
Overview
Neurotransmitter release relies on Ca2+ influx through voltage-gated calcium channels (CaV2), triggered by action potentials. Reliable release necessitates CaV2 localization near primed synaptic vesicles (SV). Rab3-interacting molecule (RIM) anchors CaV2 within nanometers to SVs, via interactions between the RIM PDZ domain and the C-terminus (CT; (i.e., DDWC-COOH-like motif)) of CaV2. Recently, a novel RIM paralog (RIM-II) with identical domains to the canonical RIM (RIM-I), was discovered, yet its functions remain undetermined.While this interaction is verified in vitro in mammals, I investigated its conservation in representative species across phyla. Directed Yeast 2-Hybrid screens indicated that this interaction is retained in basal-chordates, arthropods, brachiopods, and molluscs, revealing its presence in non-mammalian metazoans. Eliminating the last four residues on CaV2 CT notably reduced interactions with RIM-I PDZ domains, highlighting their importance for RIM-CaV2 interactions. However, RIM-II did not exhibit the same interactions across phyla, suggesting functional differences between RIM-I/-II PDZ domains.
Publisher
ProQuest Dissertations & Theses
ISBN
9798380842402
