Junctate boosts phagocytosis by recruiting endoplasmic reticulum Ca2+ stores near phagosomes

Guido, Daniele; Demaurex, Nicolas; Nunes, Paula

doi:10.1242/jcs.172510

Cited by 36 publications

(61 citation statements)

References 39 publications

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“…The TagRFP‐KDEL (Guido et al . ) plasmid was used as a negative control in Ca 2+ experiments. The gating‐deficient STIM1‐F394H–mCherry was generated by site‐directed mutagenesis of STIM1–mCherry (a kind gift from Dr Matthias Seedorf, University of Heidelberg, Germany) using the 5′‐CAC ACT CTT TGG CAC CCA CCA CGT GGC CCA CAG C‐3′ (fwd F394H).…”

Section: Methodsmentioning

confidence: 99%

“…For SOCE and I CRAC evaluation, mCherry-STIM1 (gift from Prof. Richard S. Lewis, Stanford University, USA) and cyan fluorescent protein (CFP)-STIM1 (Shen et al 2011) were co-transfected with ORAI1 wild-type (WT) or mutated constructs. The TagRFP-KDEL (Guido et al 2015) plasmid was used as a negative control in Ca 2+ experiments. The gating-deficient STIM1-F394H-mCherry was generated by site-directed mutagenesis of STIM1-mCherry (a kind gift from Dr Matthias Seedorf, University of Heidelberg, Germany) using the 5 -CAC ACT CTT TGG CAC CCA CCA CGT GGC CCA CAG C-3 (fwd F394H).…”

Section: Plasmidsmentioning

confidence: 99%

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ORAI1 channel gating and selectivity is differentially altered by natural mutations in the first or third transmembrane domain

Bulla

Gyimesi

Kim

et al. 2018

The Journal of Physiology

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Key points Gain‐of‐function mutations in the highly selective Ca2+ channel ORAI1 cause tubular aggregate myopathy (TAM) characterized by muscular pain, weakness and cramping. TAM‐associated mutations in ORAI1 first and third transmembrane domain facilitate channel opening by STIM1, causing constitutive Ca2+ influx and increasing the currents evoked by Ca2+ store depletion. Mutation V107M additionally decreases the channel selectivity for Ca2+ ions and its inhibition by acidic pH, while mutation T184M does not alter the channel sensitivity to pH or to reactive oxygen species. The ORAI blocker GSK‐7975A prevents the constitutive activity of TAM‐associated channels and might be used in therapy for patients suffering from TAM. Abstract Skeletal muscle differentiation relies on store‐operated Ca2+ entry (SOCE) mediated by STIM proteins linking the depletion of endoplasmic/sarcoplasmic reticulum Ca2+ stores to the activation of membrane Ca2+‐permeable ORAI channels. Gain‐of‐function mutations in STIM1 or ORAI1 isoforms cause tubular aggregate myopathy (TAM), a skeletal muscle disorder with muscular pain, weakness and cramping. Here, we characterize two overactive ORAI1 mutants from patients with TAM: V107M and T184M, located in the first and third transmembrane domain of the channel. When ectopically expressed in HEK‐293T cells or human primary myoblasts, the mutated channels increased basal and store‐operated Ca2+ entry. The constitutive activity of V107M, L138F, T184M and P245L mutants was prevented by low concentrations of GSK‐7975A while the G98S mutant was resistant to inhibition. Electrophysiological recordings confirmed ORAI1‐V107M constitutive activity and revealed larger STIM1‐gated V107M‐ and T184M‐mediated currents with conserved fast and slow Ca2+‐dependent inactivation. Mutation V107M altered the channel selectivity for Ca2+ ions and conferred resistance to acidic inhibition. Ca2+ imaging and molecular dynamics simulations showed a preserved sensitivity of T184M to the negative regulation by reactive oxygen species. Both mutants were able to mediate SOCE in Stim1−/−/Stim2−/− mouse embryonic fibroblasts expressing the binding‐deficient STIM1‐F394H mutant, indicating a higher sensitivity for STIM1‐mediated gating, with ORAI1‐T184M gain‐of‐function being strictly dependent on STIM1. These findings provide new insights into the permeation and regulatory properties of ORAI1 mutants that might translate into therapies against diseases with gain‐of‐function mutations in ORAI1.

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Section: Methodsmentioning

confidence: 99%

Section: Plasmidsmentioning

confidence: 99%

ORAI1 channel gating and selectivity is differentially altered by natural mutations in the first or third transmembrane domain

Bulla

Gyimesi

Kim

et al. 2018

The Journal of Physiology

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“…Additionally, 2 studies have interfered genetically with ER Ca 2+ channels to blunt this response . The Ca 2+ oscillations recorded at the late stages of phagosome maturation (30‐90 min post‐internalization) can be abolished by blocking Ins(1,4,5)P 3 receptors, or curiously, by direct interference with ER/phagosome contacts by knocking out STIM1, STIM2 or Orai1 …”

Section: Ca2+ Stores and Channels Essential To Phagosome Maturationmentioning

confidence: 99%

Revisiting the role of calcium in phagosome formation and maturation

Westman

Grinstein

Maxson

2019

Journal of Leukocyte Biology

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Like other membrane receptor-mediated responses, execution of phagocytosis requires the transduction of signals to cytoplasmic effectors. Signaling in this case is particularly complex as the process involves not only the formation of phagosomes but also their subsequent maturation and resolution. Transient increases in cytosolic calcium, which mediate a variety of other transduction pathways, also feature prominently in phagocytosis. However, despite intensive study over the course of nearly 30 years, the occurrence, source, and functional relevance of such calcium bursts remain the subject of debate. Here, we have attempted to consolidate the information that was reviewed in the past with more recent studies in an effort to shed some light on the existing controversies. K E Y W O R D Sfluorescence, calcium, phagocytosis, phagosome maturation, membrane fusion summarized in Table 1 upward of 80% of the studies reported that an elevation in [Ca 2+ ] cyt accompanied phagosome formation. Yet a significant

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“…Both junctate and STIM1 are involved in the formation of the junctions between the ER and phagosomes and, interestingly, support different forms of localised Ca 2+ responses [62, 124]. …”

Section: Junctions Between Cellular Organellesmentioning

confidence: 99%

Mitochondrial junctions with cellular organelles: Ca2+ signalling perspective

Tepikin

2018

Pflugers Arch - Eur J Physiol

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Cellular organelles form multiple junctional complexes with one another and the emerging research area dealing with such structures and their functions is undergoing explosive growth. A new research journal named “Contact” has been recently established to facilitate the development of this research field. The current consensus is to define an organellar junction by the maximal distance between the participating organelles; and the gap of 30 nm or less is considered appropriate for classifying such structures as junctions or membrane contact sites. Ideally, the organellar junction should have a functional significance, i.e. facilitate transfer of calcium, sterols, phospholipids, iron and possibly other substances between the organelles (Carrasco and Meyer in Annu Rev Biochem 80:973–1000, 2011; Csordas et al. in Trends Cell Biol 28:523–540, 2018; Phillips and Voeltz in Nat Rev Mol Cell Biol 17:69–82, 2016; Prinz in J Cell Biol 205:759–769, 2014). It is also important to note that the junction is not just a result of a random organelle collision but have active and specific formation, stabilisation and disassembly mechanisms. The nature of these mechanisms and their role in physiology/pathophysiology are the main focus of an emerging research field. In this review, we will briefly describe junctional complexes formed by cellular organelles and then focus on the junctional complexes that are formed by mitochondria with other organelles and the role of these complexes in regulating Ca2+ signalling.

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Junctate boosts phagocytosis by recruiting endoplasmic reticulum Ca2+ stores near phagosomes

Abstract: Local intracellular

Cited by 36 publications

References 39 publications

ORAI1 channel gating and selectivity is differentially altered by natural mutations in the first or third transmembrane domain

ORAI1 channel gating and selectivity is differentially altered by natural mutations in the first or third transmembrane domain

Revisiting the role of calcium in phagosome formation and maturation

Mitochondrial junctions with cellular organelles: Ca2+ signalling perspective

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