Annexin-Membrane Interactions Across Eukaryotic Domains of Life-A Comparative Approach

Abstract

This review explores the interaction of annexins with membranes across a variety of eukaryotic domains of life, highlighting this protein family's role in cellular processes due to its lipid and calcium-binding properties. By comparing annexins' functions in diverse organisms, we aim to uncover novel insights into their mechanisms of action, particularly in membrane repair, protein trafficking, and potential channel formation. Despite extensive research on mammalian and plant annexins, there is limited information on annexins in invertebrates, fungi, and protists. This review seeks to bridge this knowledge gap, providing a comprehensive understanding of annexin-membrane interactions and their potential implications for cellular function and disease mechanisms across eukaryotic lineages.

Keywords: animal; annexin; eukaryote; evolution; free-living; interaction; ion channel; lipid; membrane; membrane trafficking; parasite; plant; protist.

Figure 1

A graphical representation of a generic annexin structure with four signature domains (D1–D4), focusing on the diversity of N-terminal head domains. The figure highlights the annexins discussed in this review. Sequence information and predicted domain organization were extracted from UniProt.

Figure 2

Possible and confirmed interactions, and (putative) functions, of annexins across various biological kingdoms. Information extracted and schematized from several sources [2,4,12,15,28,30,31,34,35,36,37,39,41,43,45,46,47,48,49,50,51,52,53,54,55].