Complexin Membrane Interactions: Implications for Synapse Evolution and Function. Review uri icon

Overview

abstract

  • The molecules and mechanisms behind chemical synaptic transmission have been explored for decades. For several of the core proteins involved in synaptic vesicle fusion, we now have a reasonably detailed grasp of their biochemical, structural, and functional properties. Complexin is one of the key synaptic proteins for which a simple mechanistic understanding is still lacking. Living up to its name, this small protein has been associated with a variety of roles differing between synapses and between species, but little consensus has been reached on its fundamental modes of action. Much attention has been paid to its deeply conserved SNARE-binding properties, while membrane-binding features of complexin and their functional significance have yet to be explored to the same degree. In this review, we summarize the known membrane interactions of the complexin C-terminal domain and their potential relevance to its function, synaptic localization, and evolutionary history.

publication date

  • August 3, 2022

Research

keywords

  • Adaptor Proteins, Vesicular Transport
  • Membrane Fusion
  • Nerve Tissue Proteins
  • Synaptic Vesicles

Identity

PubMed Central ID

  • PMC9807284

Scopus Document Identifier

  • 85136749655

Digital Object Identifier (DOI)

  • 10.1016/j.jmb.2022.167774

PubMed ID

  • 35931110

Additional Document Info

volume

  • 435

issue

  • 1