Bcl-2 family in inter-organelle modulation of calcium signaling; roles in bioenergetics and cell survival

Lewis, A. C.; Hayashi, Teruo; Su, Tsung‐Ping; Betenbaugh, Michael J.

doi:10.1007/s10863-013-9527-7

Cited by 53 publications

(40 citation statements)

References 121 publications

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“…Interacts with VDAC1-Because Bcl-2 and Bcl-XL modulation of the ER-mitochondrial Ca 2ϩ transfer is likely occurring at the close contact sites between these two organelles (11), we therefore assessed whether VDAC1, IP 3 Rs, Bcl-2, and Bcl-XL localize at the MAMs as anticipated or indicated by previous studies (1,40,41). The immunoblotting results ( Fig.…”

Section: Bh4 Domain Of Bcl-xl But Not That Of Bcl-2 Specificallymentioning

confidence: 74%

The BH4 Domain of Anti-apoptotic Bcl-XL, but Not That of the Related Bcl-2, Limits the Voltage-dependent Anion Channel 1 (VDAC1)-mediated Transfer of Pro-apoptotic Ca2+ Signals to Mitochondria

Monaco

Decrock

Arbel

et al. 2015

Journal of Biological Chemistry

111

101

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Background: VDAC1 mediates the transfer of pro-apoptotic Ca 2ϩ signals into mitochondria. Results: The BH4 domain of Bcl-XL, but not that of Bcl-2, targets VDAC1 and suppresses its pro-apoptotic Ca 2ϩ -flux properties. N-terminal VDAC1 peptide alleviates this effect of BH4-Bcl-XL. Conclusion: Bcl-XL via its BH4 domain inhibits VDAC1 activity. Significance: Bcl-2 and Bcl-XL differ in their BH4 domain biology by regulating ER and mitochondrial Ca 2ϩ -transport systems, respectively.

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Section: Bh4 Domain Of Bcl-xl But Not That Of Bcl-2 Specificallymentioning

confidence: 74%

The BH4 Domain of Anti-apoptotic Bcl-XL, but Not That of the Related Bcl-2, Limits the Voltage-dependent Anion Channel 1 (VDAC1)-mediated Transfer of Pro-apoptotic Ca2+ Signals to Mitochondria

Monaco

Decrock

Arbel

et al. 2015

Journal of Biological Chemistry

111

101

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“…2B) [41]. Bcl-2-related proteins are localized to the ER [42], bind to the IP 3 Rs [43] and regulate the ER-mediated cell viability via IICR modulation [44]. Recent studies have shown that the Bcl-2 homology (BH) 4 domain of Bok binds constitutively to the residues 1895-1903 of the coupling domain of the IP 3 R and this binding is very potent (Fig.…”

Section: Structure Function and Regulation Of Ip 3 Rsmentioning

confidence: 99%

Inositol 1,4,5‐trisphosphate receptors and neurodegenerative disorders

Egorova

Bezprozvanny

2018

The FEBS Journal

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The inositol 1,4,5-trisphosphate receptor (IP 3 R) is an intracellular ion channel that mediates the release of calcium ions from the endoplasmic reticulum. It plays a role in basic biological functions, such as cell division, differentiation, fertilization and cell death, and is involved in developmental processes including learning, memory and behavior. Deregulation of neuronal calcium signaling results in disturbance of cell homeostasis, synaptic loss and dysfunction, eventually leading to cell death. Three IP 3 R subtypes have been identified in mammalian cells and the predominant isoform in neurons is IP 3 R type 1. Dysfunction of IP 3 R type 1 may play a role in the pathogenesis of certain neurodegenerative diseases as enhanced activity of the IP 3 R was observed in models of Huntington's disease, spinocerebellar ataxias and Alzheimer's disease. These results suggest that IP 3 R-mediated signaling is a potential target for treatment of these disorders. In this review we discuss the structure, functions and regulation of the IP 3 R in healthy neurons and in conditions of neurodegeneration. IntroductionInositol 1,4,5-trisphosphate receptors (IP 3 Rs) are a family of intracellular ion channels that mediate calcium (Ca 2+ ) release from the endoplasmic reticulum (ER) following stimulation by the second messenger inositol 1,4,5-trisphosphate (IP 3 ). Generation of IP 3 molecules is caused by the activation of phospholipase C in response to the activation of G proteincoupled receptors such as serotonergic receptors, adrenergic receptors, calcitonin receptors, histamine receptors, metabotropic glutamate receptors (mGluRs), Abbreviations AAV, adeno-associated virus; AD, Alzheimer's disease; ALG-2, apoptosis-linked gene 2; ARM, armadillo; Ab, beta amyloid; BH, Bcl-2 homology; CaBP1, calcium-binding protein 1; CTD, C-terminal domain; EM, electron microscopy; ER, endoplasmic reticulum; FAD, familial Alzheimer's disease; GRP78, 78-kDa glucose regulated protein; HAP1, huntingtin-associated protein 1; HD, Huntington's disease; HelD, helical domain; Htt, huntingtin; IBC, IP 3 -binding core; IICR, inositol 1,4,5-trisphosphate-induced calcium release; ILD, 'intervening lateral' domain; IP 3 , inositol 1,4,5-trisphosphate; IP 3 R1, IP 3 R type 1; IP 3 R, inositol 1,4,5-trisphosphate receptor; IRBIT, IP 3 R binding protein released with IP 3 ; KO, knock-out; LBD, ligand-binding domain; LNK, helical linker domain; MCI, mild cognitive impairment; mGluR, metabotropic glutamate receptor; mPTP, mitochondrial permeability transition pore; MSN, medium spiny neuron; NMDA, N-methyl-D-aspartate; NTR, Nterminal region; Opt, opisthotonos; PC, Purkinje cell; polyQ, polyglutamine; PS, presenilin; RyR, ryanodine receptor; SAD, sporadic Alzheimer's disease; SCA, spinocerebellar ataxia; SD, IP 3 -binding suppressor domain; SUMF1, sulfatase modifying factor 1; TG2, transglutaminase type 2; TMD, transmembrane domain; WT, wild-type; YAC, yeast artificial chromosome; b-TF, b-trefoil. 3547The (Fig. 1). Upon extracellular stimulation -by various ...

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“…Bcl-2 prevents Ca 2+ release from the ER by binding to the BH4 domain in IP3R and RyR, and inhibiting their activities [25]. In cadmium-treated cerebral cortical neurons cells, cadmium decreases Bcl-2 and increases Bax, promoting Ca 2+ overload and triggering cell apoptosis [26].…”

Section: Mechanisms Of Ca 2+ Overload-mediated Cell Apoptosis Inducedmentioning

confidence: 99%

Calcium Homeostasis Disruption - a Bridge Connecting Cadmium-Induced Apoptosis, Autophagy and Tumorigenesis

et al. 2015

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Calcium and cadmium are divalent metals and have similar chemical properties. Both can enter cells through, albeit different, channels, or through protein-dependent permeation. However, cadmium disturbs the calcium homeostasis by inhibiting calcium channels and/or related proteins. Cadmium can also alter membrane phospholipid concentrations, and so induce a calcium homeostasis disorder. The altered calcium homeostasis induced by cadmium results in cell apoptosis, autophagy or tumorigenesis. In this review, calcium homeostasis disruption is summarized as a bridge connecting cadmium-induced apoptosis, autophagy, and tumorigenesis.

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Bcl-2 family in inter-organelle modulation of calcium signaling; roles in bioenergetics and cell survival

Cited by 53 publications

References 121 publications

The BH4 Domain of Anti-apoptotic Bcl-XL, but Not That of the Related Bcl-2, Limits the Voltage-dependent Anion Channel 1 (VDAC1)-mediated Transfer of Pro-apoptotic Ca2+ Signals to Mitochondria

The BH4 Domain of Anti-apoptotic Bcl-XL, but Not That of the Related Bcl-2, Limits the Voltage-dependent Anion Channel 1 (VDAC1)-mediated Transfer of Pro-apoptotic Ca2+ Signals to Mitochondria

Inositol 1,4,5‐trisphosphate receptors and neurodegenerative disorders

Calcium Homeostasis Disruption - a Bridge Connecting Cadmium-Induced Apoptosis, Autophagy and Tumorigenesis

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