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Hoogstraaten, R. I.

Publications and source records attributed to Hoogstraaten, R. I..

2 recordsLinked to original sources

ER Ca2+-levels control neuromodulator secretion by regulating STIM1 and L-type Ca2+-channel activity

AbstractRegulated secretion is typically triggered by (local) increases in intracellular Ca2+, but the source of Ca2+, influx through voltage gated Ca2+ channels or release from the endoplasmic reticulum (ER), has distinct effects, particularly for neuropeptide secretion from dense-core vesicles (DCVs). Here, we show that in primary mouse neurons acute ER Ca2+ depletion by caffeine, cyclopiazonic acid or thapsigargin resulted in minute increases in bulk cytosolic free Ca2+ ([Ca2+]bulk) that did not trigger significant DCV exocytosis. Remarkably, following acute ER Ca2+ depletion, action potential (AP) trains triggered 50-90% less DCV exocytosis as compared to naive neurons. In contrast, synaptic vesicle (SV) exocytosis was similar with/without acute ER Ca2+ depletion. Unexpectedly, acute ER Ca2+ depletion also reduced AP-induced [Ca2+]bulk-increases. L-type Ca2+-channel inhibitor nimodipine produced similar effects: reduced [Ca2+]bulk-increase, DCV-exocytosis but not SV exocytosis, i.e., for all three parameters a phenocopy of ER depletion. Finally, introducing L-type channels lacking STIM1 interaction sites restored DCV exocytosis following ER store depletion. We conclude that in mouse neurons, acute ER Ca2+ release is not effective in releasing neuromodulators. Instead, ER depletion activates a STIM1-dependent negative feedback loop that inhibits L-type Ca2+ channel activity, essential for DCV- but not SV-exocytosis.

neuroscience↗

Rabphilin-3A negatively regulates neuropeptide release, through its SNAP25 interaction

Neuropeptides and neurotrophins are stored in and released from dense-core vesicles (DCVs). While DCVs and synaptic vesicles (SVs) share fundamental SNARE/SM proteins for exocytosis, a detailed understanding of DCV exocytosis remains elusive. We recently identified the RAB3-RIM1 pathway to be essential for DCV-, but not SV exocytosis, highlighting a significant distinction between the SV- and DCV secretory pathways. Whether RIM1 is the only RAB3 effector that is essential for DCV exocytosis is currently unknown. In this study, we show that rabphilin-3A (RPH3A), a known downstream effector of RAB3A, is a negative regulator of DCV exocytosis. Using live-cell imaging at single vesicle resolution with RPH3A-deficient hippocampal neurons, we show that DCV exocytosis increased 3-fold in the absence of RPH3A. RAB3A-binding deficient RPH3A lost its punctate distribution, but still restored DCV exocytosis to WT levels when re-expressed. SNAP25-binding deficient RPH3A did not rescue DCV exocytosis. In addition, we show that RPH3A did not travel with DCVs, but remained stationary at pre-synapses. RPH3A null neurons also had longer neurites, which was partly restored when ablating all regulated secretion with tetanus neurotoxin. Taken together, these results show that RPH3A negatively regulates DCV exocytosis, potentially also affecting neuron size. Furthermore, RAB3A interaction is required for the synaptic enrichment of RPH3A, but not for limiting DCV exocytosis. Instead, the interaction of RPH3A with SNAP25 is relevant for inhibiting DCV exocytosis.

neuroscience↗