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Review
. 2007 Dec 15;585(Pt 3):687-91.
doi: 10.1113/jphysiol.2007.137539. Epub 2007 Jun 21.

Activity-dependent control of bulk endocytosis by protein dephosphorylation in central nerve terminals

Emma L Clayton  1 , Gareth J O Evans, Michael A Cousin
Affiliations
Review

Activity-dependent control of bulk endocytosis by protein dephosphorylation in central nerve terminals

Emma L Clayton et al. J Physiol. .

Abstract

Bulk endocytosis is the process by which nerve terminals retrieve large amounts of synaptic vesicle membrane during periods of strong stimulation intensity. The process is rapidly activated and is most probably calcium dependent in a similar manner to synaptic vesicle exocytosis. This article briefly summarizes the current knowledge of bulk endocytosis with respect to its activation, kinetics and molecular mechanism. It also presents recent data from our laboratory showing that the dephosphorylation of a group of endocytosis proteins called the dephosphins by the Ca(2+)-dependent protein phosphatase calcineurin is key to the activity-dependent stimulation of the process. Possible downstream effectors of calcineurin are discussed such as the large GTPase dynamin I and its phosphorylation-dependent interaction partner syndapin I.

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Figures

Figure 1
Figure 1. Multiple synaptic vesicle retrieval pathways in central nerve terminals
Three different mechanisms are propsed to retrieve synaptic vesicle (SV) membrane after exocytosis in nerve terminals. Kiss-and-run is a mechanism where the SV never fully fuses with the plasma membrane and retrieves intact. Classical clathrin-dependent endocytosis involves the invagination of a single clathrin-coated bud from the plasma membrane before its fission and uncoating. Bulk endocytosis is the process where large areas of nerve terminal membrane are invaginated to produce endosomes from which SVs can bud.
See this image and copyright information in PMC

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