Lessons from the Endoplasmic Reticulum Ca2+ Transporters—A Cancer Connection

Zhai, Xingjian; Sterea, Andra M.; Hiani, Yassine El

doi:10.3390/cells9061536

Cited by 21 publications

(18 citation statements)

References 198 publications

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“…MCSs allows the efficient transfer of metabolites between compartments, particularly of calcium. The cytosol calcium concentrations are ∼100 nM ( Marchi et al, 2020 ), whereas in the ER lumen [(Ca 2+ ) ER ], it reaches 100–800 μM ( Burdakov et al, 2005 ; Zhai et al, 2020 ).…”

Section: Regulated Cellular Processes At Contact Sites and Their Relamentioning

confidence: 99%

Relevance of Membrane Contact Sites in Cancer Progression

Gil-Hernández

Arroyo-Campuzano

Simoni‐Nieves

et al. 2021

Front. Cell Dev. Biol.

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Membrane contact sites (MCS) are typically defined as areas of proximity between heterologous or homologous membranes characterized by specific proteins. The study of MCS is considered as an emergent field that shows how crucial organelle interactions are in cell physiology. MCS regulate a myriad of physiological processes such as apoptosis, calcium, and lipid signaling, just to name a few. The membranal interactions between the endoplasmic reticulum (ER)–mitochondria, the ER–plasma membrane, and the vesicular traffic have received special attention in recent years, particularly in cancer research, in which it has been proposed that MCS regulate tumor metabolism and fate, contributing to their progression. However, as the therapeutic or diagnostic potential of MCS has not been fully revisited, in this review, we provide recent information on MCS relevance on calcium and lipid signaling in cancer cells and on its role in tumor progression. We also describe some proteins associated with MCS, like CERT, STIM1, VDAC, and Orai, that impact on cancer progression and that could be a possible diagnostic marker. Overall, these information might contribute to the understanding of the complex biology of cancer cells.

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Section: Regulated Cellular Processes At Contact Sites and Their Relamentioning

confidence: 99%

Relevance of Membrane Contact Sites in Cancer Progression

Gil-Hernández

Arroyo-Campuzano

Simoni‐Nieves

et al. 2021

Front. Cell Dev. Biol.

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“…Depending on the context, the increase in [Ca 2+ ]i exerts either pro-apoptotic or anti-apoptotic roles [ 43 , 44 ]. For example, it was shown that CD95- or TRAIL-mediated Ca 2+ release led to apoptosis resistance due to delayed DISC formation [ 38 ] or TRAIL–DR endocytosis, respectively [ 25 ].…”

Section: Resultsmentioning

confidence: 99%

TRAIL Triggers CRAC-Dependent Calcium Influx and Apoptosis through the Recruitment of Autophagy Proteins to Death-Inducing Signaling Complex

Airiau

Vacher

Micheau

et al. 2021

Cells

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Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) selectively kills various cancer cell types, but also leads to the activation of signaling pathways that favor resistance to cell death. Here, we investigated the as yet unknown roles of calcium signaling and autophagy regulatory proteins during TRAIL-induced cell death in leukemia cells. Taking advantage of the Gene Expression Profiling Interactive Analysis (GEPIA) project, we first found that leukemia patients present a unique TRAIL receptor gene expression pattern that may reflect their resistance to TRAIL. The exposure of NB4 acute promyelocytic leukemia cells to TRAIL induces intracellular Ca2+ influx through a calcium release-activated channel (CRAC)-dependent mechanism, leading to an anti-apoptotic response. Mechanistically, we showed that upon TRAIL treatment, two autophagy proteins, ATG7 and p62/SQSTM1, are recruited to the death-inducing signaling complex (DISC) and are essential for TRAIL-induced Ca2+ influx and cell death. Importantly, the treatment of NB4 cells with all-trans retinoic acid (ATRA) led to the upregulation of p62/SQSTM1 and caspase-8 and, when added prior to TRAIL stimulation, significantly enhanced DISC formation and the apoptosis induced by TRAIL. In addition to uncovering new pleiotropic roles for autophagy proteins in controlling the calcium response and apoptosis triggered by TRAIL, our results point to novel therapeutic strategies for sensitizing leukemia cells to TRAIL.

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“…In all these instances, metabolic rewiring is coupled with modifications of Ca 2+ fluxes, particularly those involving the ER Ca 2+ store ( Zhai et al, 2020 ). It has been described that pancreatic ( Okeke et al, 2016 ), breast ( Singh et al, 2017 ), colorectal ( Pierro et al, 2014 ), glioblastoma ( Kang et al, 2017 ), gastric ( Sakakura et al, 2003 ), and lung cancers ( Bergner et al, 2009 ) show increases in IP3R isoform levels, IP3R3 being the preponderant isoform ( Rezuchova et al, 2019 ; Rosa et al, 2020 ), followed by IP3R2 ( Vervloessem et al, 2014 ; Bartok et al, 2019 ).…”

Section: Implications In Cancermentioning

confidence: 99%

In the Right Place at the Right Time: Regulation of Cell Metabolism by IP3R-Mediated Inter-Organelle Ca2+ Fluxes

Ahumada-Castro

Bustos

Silva-Pavez

et al. 2021

Front. Cell Dev. Biol.

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In the last few years, metabolism has been shown to be controlled by cross-organelle communication. The relationship between the endoplasmic reticulum and mitochondria/lysosomes is the most studied; here, inositol 1,4,5-triphosphate (IP3) receptor (IP3R)-mediated calcium (Ca2+) release plays a central role. Recent evidence suggests that IP3R isoforms participate in synthesis and degradation pathways. This minireview will summarize the current findings in this area, emphasizing the critical role of Ca2+ communication on organelle function as well as catabolism and anabolism, particularly in cancer.

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Lessons from the Endoplasmic Reticulum Ca2+ Transporters—A Cancer Connection

Cited by 21 publications

References 198 publications

Relevance of Membrane Contact Sites in Cancer Progression

Relevance of Membrane Contact Sites in Cancer Progression

TRAIL Triggers CRAC-Dependent Calcium Influx and Apoptosis through the Recruitment of Autophagy Proteins to Death-Inducing Signaling Complex

In the Right Place at the Right Time: Regulation of Cell Metabolism by IP3R-Mediated Inter-Organelle Ca2+ Fluxes

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