Membrane shaping by actin and myosin during regulated exocytosis
Abstract The cortical actin network in neurosecretory cells is a dense mesh of actin filaments underlying the plasma membrane. Interaction of actomyosin with vesicular membranes or the plasma membrane is vital for tethering, retention, transport as well as fusion and fission of exo- and endocytic membrane structures. During regulated exocytosis the cortical actin network undergoes dramatic changes in morphology to accommodate vesicle docking, fusion and replenishment. Most of these processes involve plasma membrane Phosphoinositides (PIP) and investigating the interactions between the actin cortex and secretory structures has become a hotbed for research in recent years. Actin remodelling leads to filopodia outgrowth and the creation of new fusion sites in neurosecretory cells and actin, myosin and dynamin actively shape and maintain the fusion pore of secretory vesicles. Changes in viscoelastic properties of the actin cortex can facilitate vesicular transport and lead to docking and priming of vesicle at the plasma membrane. Small GTPase actin mediators control the state of the cortical actin network and influence vesicular access to their docking and fusion sites. These changes potentially affect membrane properties such as tension and fluidity as well as the mobility of embedded proteins and could influence the processes leading to both exo- and endocytosis. Here we discuss the multitudes of actin and membrane interactions that control successive steps underpinning regulated exocytosis. Highlights Cortical actin network interaction with membranes of the exocytotic pathway regulates hormone and neurotransmitter release. Activity dependent actomyosin cortex remodeling directs vesicles toward docking sites and generates de novo release sites. Actin, myosin and dynamin regulate opening, stability and duration of the fusion pore, fine-tuning neurotransmitter release. Small ATPases, Phosphoinositides and F-actin work together to link secretory vesicles to the plasma membrane.
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