Syndapin I is the phosphorylation-regulated dynamin I partner in synaptic vesicle endocytosis

Anggono, Victor; Smillie, Karen J.; Graham, Mark E.; Valova, Valentina A.; Cousin, Michael A.; Robinson, Phillip J.

doi:10.1038/nn1695

Cited by 195 publications

(312 citation statements)

References 40 publications

Supporting

Mentioning

302

Contrasting

Order By: Relevance

“…Bulk-like endocytosis is activated by strong stimulation in neurons (Clayton et al, 2008). In parallel, elevated Ca 2+ activates the calcium/calmodulin -dependent protein phosphatase calcineurin, which leads to the dephosphorylation of dynamin I and its interaction with the F-BAR protein, syndapin I (Anggono et al, 2006;. Therefore, our data appear to agree with the specific role of dynamin I rephosphorylation at SER-774 in bulk-like endocytosis in neurons (Clayton et al, 2010).…”

Section: Disscusionsupporting

confidence: 86%

Bulk-like endocytosis plays an important role in the recycling of insulin granules in pancreatic beta cells

Xue

Yuan

et al. 2012

Protein Cell

View full text Add to dashboard Cite

Although bulk endocytosis has been found in a number of neuronal and endocrine cells, the molecular mechanism and physiological function of bulk endocytosis remain elusive. In pancreatic beta cells, we have observed bulk-like endocytosis evoked both by flash photolysis and trains of depolarization. Bulk-like endocytosis is a clathrin-independent process that is facilitated by enhanced extracellular Ca 2+ entry and suppressed by the inhibition of dynamin function. Moreover, defects in bulklike endocytosis are accompanied by hyperinsulinemia in primary beta cells dissociated from diabetic KKAy mice, which suggests that bulk-like endocytosis plays an important role in maintaining the exo-endocytosis balance and beta cell secretory capability.

show abstract

Section: Disscusionsupporting

confidence: 86%

Bulk-like endocytosis plays an important role in the recycling of insulin granules in pancreatic beta cells

Xue

Yuan

et al. 2012

Protein Cell

View full text Add to dashboard Cite

show abstract

“…Block of dynamin I function has no effect on the final endosomal scission step under elevated stimulation conditions where a dynamin II and clathrin mediated process predominates in adrenal chromaffin cells [4,22]. This seems not to extend to neuronal preparations where dynamin I seems to be directly associated with clathrin-mediated internalization of small, clear vesicle membrane [46][47][48] where it is activated under elevated stimulus conditions [26,[49][50][51]. This point is of note for several reasons.…”

Section: Discussionmentioning

confidence: 98%

Dynamin I plays dual roles in the activity-dependent shift in exocytic mode in mouse adrenal chromaffin cells

Fulop

Doreian

Smith

2008

Archives of Biochemistry and Biophysics

View full text Add to dashboard Cite

Under low stimulation, adrenal chromaffin cells release freely-soluble catecholamines through a restricted granule fusion pore while retaining the large neuropeptide-containing proteinacious granule core. Elevated activity causes dilation of the pore and release of all granule contents. Thus, physiological differential transmitter release is achieved through regulation of fusion pore dilation. We examined the mechanism for pore dilation utilizing a combined approach of peptide transfection, electrophysiology, electrochemistry and quantitative imaging techniques. We report that disruption of dynamin I function alters both fusion modes. Under low stimulation, interference with dynamin I does not affect granule fusion but blocks its re-internalization. In full collapse mode, disruption of dynamin I limits fusion pore dilation, but does not block membrane re-internalization. These data suggest that dynamin I is involved in both modes of exocytosis by regulating contraction or dilation of the fusion pore and thus contributes to activity-dependent differential transmitter release from the adrenal medulla.

show abstract

“…Calmodulin also mediates rapid recruitment of fast-releasing synaptic vesicles at the calyx of Held 97,98 , further underlining the intimate connection between presynaptic Ca 2+ , release site clearance and endocytosis. other Ca 2+ -binding proteins, such as calcineurin 87,88,99,100 , synaptotagmins, complexins or Munc13 (REFS 12,101) might be additional Ca 2+ effectors facilitating exocytic-endocytic coupling.…”

Section: Calcium Regulationmentioning

confidence: 99%

Protein scaffolds in the coupling of synaptic exocytosis and endocytosis

2011

View full text Add to dashboard Cite

Communication between nerve cells largely occurs at chemical synapses -specialized sites of cell-cell contact where electrical signals trigger the exocytic release of neurotransmitter, which in turn activates postsynaptic receptor channels. The efficacy with which such chemical signals are transmitted is crucial for the functioning of the nervous system. Modulation of neurotransmission enables nerve cells to respond to a vast range of stimulus patterns. Synaptic activity can also be tremendously diverse; from the fast synapses of the hippocampus, to slow neuropeptide-containing synapses. Indeed, some signalling pathways are active in the absence of stimulation, such as those involved in the processing of sensory information, which transmit tonically at high rates of up to 100 Hz or more 1,2 .Intriguing questions arise from these facts, including how high rates of neurotransmission can be maintained over long periods of time, and what limits the ability of a given synapse to release neurotransmitter during sustained periods of activity. Recent data indicate that in many synapses, exocytosis of neurotransmitter is coupled to endocytosis, and that synapses have evolved a specialized apparatus of scaffolding proteins to comply with these demands. Such scaffolds aid the temporal and spatial coupling of exocytosis and endocytosis, and are crucial for maintaining rapid neurotransmission during sustained activity 3 .Exocytosis of neurotransmitter is triggered by stimulusinduced calcium influx into the nerve terminal 4,5 and the subsequent fusion of synaptic vesicles with the presynaptic plasma membrane at specialized regions called active zones (BOX 1). Exocytosed synaptic vesicle membrane proteins and lipids in turn are recycled at the endocytic or periactive zone (BOX 1) that surrounds the release site, to restore functional synaptic vesicle pools for reuse and to ensure long-term functionality of the synapse 6-8 (FIG. 1). Depending on the type of synapse and the stimulation frequency, several modes of endocytosis with different time constants -for example, fast and slow endocytosisseem to operate 7,9,10 . Clathrin-mediated endocytosis arguably represents the main pathway of synaptic vesicle endocytosis 6,8,11 , although other modes -for example, fast kiss-and-run exocytosis and endocytosis -could operate in parallel.Although the machineries for exocytic membrane fusion 12,13 and for endocytic retrieval of synaptic vesicle membranes have been studied separately in some detail 6,14 , comparatively little is known about the coupling between exocytosis and endocytosis. Here we synthesize recent data from physiological, morphological and biochemical studies in several model systems into hypothetical models for scaffold-based mechanisms underlying exocytic-endocytic coupling.The synaptic vesicle cycle Synaptic vesicle pools. Some defining features of chemical synapses are the presence of one or several clusters of synaptic vesicles in the presynaptic nerve terminal, and ultrastructural specializations at the pre-and postsy...

show abstract

Syndapin I is the phosphorylation-regulated dynamin I partner in synaptic vesicle endocytosis

Cited by 195 publications

References 40 publications

Bulk-like endocytosis plays an important role in the recycling of insulin granules in pancreatic beta cells

Bulk-like endocytosis plays an important role in the recycling of insulin granules in pancreatic beta cells

Dynamin I plays dual roles in the activity-dependent shift in exocytic mode in mouse adrenal chromaffin cells

Protein scaffolds in the coupling of synaptic exocytosis and endocytosis

Contact Info

Product

Resources

About