Exocytosis and Endocytosis in Neuroendocrine Cells: Inseparable Membranes!

Houy, Sébastien; Croisé, Pauline; Gubar, Olga; Chasserot‐Golaz, Sylvette; Tryoen-Tóth, Petra; Bailly, Yannick; Ory, Stéphane; Bader, Marie‐France; Gasman, Stéphane

doi:10.3389/fendo.2013.00135

Cited by 32 publications

(20 citation statements)

References 56 publications

(64 reference statements)

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“…Thus, we employed adrenal chromaffin cells, a well-established model to study calcium-regulated exocytosis, given that these cells use similar molecular machinery as neurons 33,34 . After LDCVs fuse with the plasma membrane in chromaffin cells, an orchestrated process of compensatory endocytosis efficiently removes the added membrane and proteins, and delivers them to a near-Golgi area, a process that takes tens of minutes 35 . We found that chromaffin cells, like neurons, contain mRNAs for all three endophilins.…”

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confidence: 99%

Endophilin-A coordinates priming and fusion of neurosecretory vesicles via intersectin

et al. 2020

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Endophilins-A are conserved endocytic adaptors with membrane curvature-sensing and -inducing properties. We show here that, independently of their role in endocytosis, endophilin-A1 and endophilin-A2 regulate exocytosis of neurosecretory vesicles. The number and distribution of neurosecretory vesicles were not changed in chromaffin cells lacking endophilin-A, yet fast capacitance and amperometry measurements revealed reduced exocytosis, smaller vesicle pools and altered fusion kinetics. The levels and distributions of the main exocytic and endocytic factors were unchanged, and slow compensatory endocytosis was not robustly affected. Endophilin-A's role in exocytosis is mediated through its SH3domain, specifically via a direct interaction with intersectin-1, a coordinator of exocytic and endocytic traffic. Endophilin-A not able to bind intersectin-1, and intersectin-1 not able to bind endophilin-A, resulted in similar exocytic defects in chromaffin cells. Altogether, we report that two endocytic proteins, endophilin-A and intersectin-1, are enriched on neurosecretory vesicles and regulate exocytosis by coordinating neurosecretory vesicle priming and fusion.

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confidence: 99%

Endophilin-A coordinates priming and fusion of neurosecretory vesicles via intersectin

et al. 2020

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“…Hence, exo‐endocytosis coupling leads then to recycling of post‐exocytotic internalized granule membrane back to the Golgi apparatus, starting a new life for the secretory granule (Houy et al . ). Recently lipids generated upon exocytosis have been proposed to contribute to the exo‐endocytosis coupling (Yuan et al .…”

Section: Lipids and Exocytosis Of Secretory Granulesmentioning

confidence: 97%

“…Molecular mechanisms underlying the preservation of granule mem- brane identity after fusion with plasma membrane remains unclear, but it has been proposed that specific lipid microdomains might contribute to prevent diffusion of granular components. Hence, exo-endocytosis coupling leads then to recycling of post-exocytotic internalized granule membrane back to the Golgi apparatus, starting a new life for the secretory granule (Houy et al 2013). Recently lipids generated upon exocytosis have been proposed to contribute to the exo-endocytosis coupling (Yuan et al 2015).…”

Section: Lipids Regulating Molecular Mechanisms Of Priming Stepsmentioning

confidence: 99%

Lipids implicated in the journey of a secretory granule: from biogenesis to fusion

Tanguy

Carmon

Wang

et al. 2016

Journal of Neurochemistry

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The regulated secretory pathway begins with the formation of secretory granules by budding from the Golgi apparatus and ends by their fusion with the plasma membrane leading to the release of their content into the extracellular space, generally following a rise in cytosolic calcium. Generation of these membrane-bound transport carriers can be classified into three steps: (i) cargo sorting that segregates the cargo from resident proteins of the Golgi apparatus, (ii) membrane budding that encloses the cargo and depends on the creation of appropriate membrane curvature, and (iii) membrane fission events allowing the nascent carrier to separate from the donor membrane. These secretory vesicles then mature as they are actively transported along microtubules toward the cortical actin network at the cell periphery. The final stage known as regulated exocytosis involves the docking and the priming of the mature granules, necessary for merging of vesicular and plasma membranes, and the subsequent partial or total release of the secretory vesicle content. Here, we review the latest evidence detailing the functional roles played by lipids during secretory granule biogenesis, recruitment, and exocytosis steps. In this review, we highlight evidence supporting the notion that lipids play important functions in secretory vesicle biogenesis, maturation, recruitment, and membrane fusion steps. These effects include regulating various protein distribution and activity, but also directly modulating membrane topology. The challenges ahead to understand the pleiotropic functions of lipids in a secretory granule's journey are also discussed. This article is part of a mini review series on Chromaffin cells (ISCCB Meeting, 2015).

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“…2) may have some relevance as endocytosis is a fundamental process of membrane recovery in neurons upon calcium-related exocytosis of secretory vesicles (Houy et al, 2013). Intracellular sequestration of ECs, which would provide an intracellular compartment that is not free to equilibrate with the extracellular AEA pool, was suggested .…”

Section: Model Of Endocytosis-mediated Aea Uptake and Intracellularmentioning

confidence: 99%

Endocannabinoid Transport Revisited

Nicolussi

Gertsch

2015

Vitamins &Amp; Hormones

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Exocytosis and Endocytosis in Neuroendocrine Cells: Inseparable Membranes!

Cited by 32 publications

References 56 publications

Endophilin-A coordinates priming and fusion of neurosecretory vesicles via intersectin

Endophilin-A coordinates priming and fusion of neurosecretory vesicles via intersectin

Lipids implicated in the journey of a secretory granule: from biogenesis to fusion

Endocannabinoid Transport Revisited

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