Bulk endocytosis at neuronal synapses

Nguyen, Tam H.; Qiu, Xinwei; Sun, Jianyuan; Meunier, Frédéric A.

doi:10.1007/s11427-014-4636-z

Cited by 8 publications

(5 citation statements)

References 56 publications

(61 reference statements)

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“…We did not detect any significant difference in either F1 or F2, arguing for no apparent defects in SVR (Fig 2C, right). However, compensatory endocytic mechanisms might mask a defect in classical SVR (Nguyen et al, 2014); thus, we proceeded with an ultrastructural analysis of Eps15L1 -KO neurons. We detected a reduction of synaptic vesicles in Eps15L1 -KO synapses of about 50%, although synapses from Eps15 -KO were comparable with WT (Fig 2D).…”

Section: Resultsmentioning

confidence: 99%

Redundant and nonredundant organismal functions of EPS15 and EPS15L1

et al. 2019

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Section: Resultsmentioning

confidence: 99%

Redundant and nonredundant organismal functions of EPS15 and EPS15L1

et al. 2019

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“…Both of these interventions will with little doubt decrease lateral membrane tension. It will now be of considerable interest to test whether inhibitory effects of actin disruption on ‘bulk endocytosis’ in neurons (62) are also dependent on lateral PM tension.…”

Section: Discussionmentioning

confidence: 99%

Constitutive Plasma Membrane Turnover in T-REx293 cells via Ordered Membrane Domain Endocytosis under Mitochondrial Control

Deisl,

Moe,

Hilgemann

2024

Preprint

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Clathrin/dynamin-independent endocytosis of ordered plasma membrane domains (ordered membrane domain endocytosis, OMDE) can be far more powerful than conventional endocytosis. Nevertheless, it remains controversial how OMDE takes place, in which cell processes it is important, and how it is regulated. Using patch clamp, we have described that OMDE becomes massive in multiple cell types in response to Ca elevations, G protein activation by non-hydrolyzable GTP analogs, and enhanced oxidative metabolism. We describe here that cytoplasmic succinate and pyruvate, but not β-hydroxybutyrate, can induce OMDE of 75% of the plasma membrane in murine marrow macrophages (BMMs) within 2 min. OMDE is decreased by 70% in BMMs lacking the acyltransferase, DHHC5, by treatment with carnitine to shift long-chain acyl groups from cytoplasmic to mitochondrial acyl-CoAs, by bromopalmitate/albumin complexes to block DHHCs, and by the cyclosporin, NIM811, to block permeability transition pores that may release mitochondrial coenzyme A into the cytoplasm. Using T-REx293 cells, plasma membrane loss amounts to 40% with pyruvate or GTPγS, whereby OMDE is then highly sensitive to actin cytoskeleton disruption. Using fluorescent 3kD dextrans to monitor constitutive endocytosis in unperturbed cells without serum or bicarbonate, multiple results suggest that OMDE is constitutively active in T-REx293 cells, but not in BMMs. In T-REx293 cells, substrates that generate metabolites activated by coenyzme A (CoA), e.g. pyruvate and hydroxybutyrate, inhibit endocytosis as expected for a shift of long-chain acyl-CoA to other CoA metabolites. In the presence of bicarbonate, however, pyruvate strongly enhances OMDE, and OMDE is then blocked by β-hydroxybutyrate, bromopalmitate/albumin complexes, and cyclosporines. After pyruvate responses, T-REx293 cells grow normally without evidence of apoptosis. Low concentrations of fatty acid (FA)-free albumin inhibit basal endocytosis in T-REx293 cells, but not BMMs, as do cyclosporines, carnitine, and RhoA blockade. However, constitutive endocytosis (i.e. in the absence of substrates and bicarbonate) is not inhibited by siRNA knockdown of the acyltransferases, DHHC5 or DHHC2, which support OMDE responses activated in patch clamp experiments. We verify biochemically that small CoA metabolites cause a decrease of long-chain acyl-CoAs and that several palmitoylated membrane proteins are depalmitoylated during treatments that decrease long-chain acyl-CoAs. STED microscopy reveals that vesicles formed in constitutive OMDE in T-REX293 cells have diameters of 90 to 130 nm. In summary, palmitoylation-dependent OMDE is likely a major G-protein-dependent endocytic mechanism that can be constitutively active, albeit not in BMMs. It depends on the activities of different DHHC acyltransferases in different cellular circumstances and can be limited by local supplies of fatty acids, CoA, and long-chain acyl-CoAs.

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“…In this issue they describe what is currently known of the molecular mechanisms underpinning the process of bulk endocytosis in a number of neuronal models [3]. Professor Sun collaborates also with Professor Pankaj Sah (QBI) on the physiology of information processing in the amygdala, the key site for emotional processing in the brain.…”

mentioning

confidence: 99%

Introduction to the thematic issue “From brain function to therapy”

Bartlett

2014

Sci. China Life Sci.

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Bulk endocytosis at neuronal synapses

Cited by 8 publications

References 56 publications

Redundant and nonredundant organismal functions of EPS15 and EPS15L1

Redundant and nonredundant organismal functions of EPS15 and EPS15L1

Constitutive Plasma Membrane Turnover in T-REx293 cells via Ordered Membrane Domain Endocytosis under Mitochondrial Control

Introduction to the thematic issue “From brain function to therapy”

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