Abstract
The cortical actin network is a mesh of filaments distributed beneath the plasmalemma that dynamically reacts in response to stimuli. This dynamic network of cortical filaments, together with motor myosin partners, adjusts the plasmalemma tension, organizes membrane protein microdomains, remodels the cell surface and drives vesicle motion in order to fine-tune exocytosis, endocytosis and recycling of secretory vesicles. In this review, we discuss how these mechanisms work in secretory cells.
Highlights
The cytoskeletal actin network is a highly dynamic mesh of filaments formed by globular actin monomers (G-actin) that assemble to form actin filaments (F-actin)
Biochemical assays in chromaffin cells, together with immunogold electron microscopy, reveal that annexin A2 is recruited to the plasmalemma upon cell stimulation, where it bundles actin filaments that organize lipid platforms for docking and exocytosis of secretory vesicles (Gabel et al, 2015)
By using membrane capacitance measurements in mouse chromaffin cells, that the fast dynamin-dependent endocytosis which develops after the exocytosis triggered by action potential-type (ETAP) stimulus (Moya-Díaz et al, 2016, 2020) depends on cortical F-actin (Montenegro et al, 2021)
Summary
The cytoskeletal actin network is a highly dynamic mesh of filaments formed by globular actin monomers (G-actin) that assemble to form actin filaments (F-actin). We will focus on the role of the cortical F-actin network on regulated exocytosis, compensatory endocytosis and vesicle recycling in secretory cells, with an emphasis on adrenal chromaffin cells.
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