Ryanodine receptors

Hamilton, Susan L.

doi:10.1016/j.ceca.2005.06.037

Cited by 123 publications

(88 citation statements)

References 88 publications

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“…This provided yet another parallel with RyR, which are also biphasically regulated by Ca 2þ (Hamilton 2005). The coregulation of IP 3 R by IP 3 and Ca 2þ in permeabilized cells was confirmed by single-channel recordings of IP 3 R1 reconstituted into lipid bilayers Striggow and Ehrlich 1996;Kaftan et al 1997;Ramos-Franco et al 1998a;Ramos-Franco et al 1998b;Tu et al 2002;Tu et al 2005b) and in native nuclear membranes (Stehno-Bittel et al 1995;Mak et al 1998;Boehning et al 2001a;Marchenko et al 2005).…”

Section: Regulation Of Ip 3 Receptors By Ca 2þ and Ipmentioning

confidence: 72%

IP3 Receptors: Toward Understanding Their Activation

Taylor¹,

Tovey²

2010

Cold Spring Harbor Perspectives in Biology

259

190

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Inositol 1,4,5-trisphosphate receptors (IP 3 R) and their relatives, ryanodine receptors, are the channels that most often mediate Ca 2þ release from intracellular stores. Their regulation by Ca 2þ allows them also to propagate cytosolic Ca 2þ signals regeneratively. This brief review addresses the structural basis of IP 3 R activation by IP 3 and Ca 2þ . IP 3 initiates IP 3 R activation by promoting Ca 2þ binding to a stimulatory Ca 2þ -binding site, the identity of which is unresolved. We suggest that interactions of critical phosphate groups in IP 3 with opposite sides of the clam-like IP 3 -binding core cause it to close and propagate a conformational change toward the pore via the adjacent N-terminal suppressor domain. The pore, assembled from the last pair of transmembrane domains and the intervening pore loop from each of the four IP 3 R subunits, forms a structure in which a luminal selectivity filter and a gate at the cytosolic end of the pore control cation fluxes through the IP 3 R.

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Section: Regulation Of Ip 3 Receptors By Ca 2þ and Ipmentioning

confidence: 72%

IP3 Receptors: Toward Understanding Their Activation

Taylor¹,

Tovey²

2010

Cold Spring Harbor Perspectives in Biology

259

190

View full text Add to dashboard Cite

show abstract

“…[83][84][85] The ER membrane is also endowed with two classes of Ca 2ϩ release channels (i.e, the Ca 2ϩ -gated Ca 2ϩ channels, generally known as ryanodine receptors, or RyRs, and Inositol 1,4,5-trisphosphate [InsP 3 ]-gated channels, or InsP 3 receptors). 86,87 Both channels are sensitive to cytosolic Ca 2ϩ (thus being able to produce Ca 2ϩ -induced Ca 2ϩ release). In addition, the InsP 3 receptors are sensitive to intracellular second messenger InsP 3 .…”

Section: Signaling In Neuronal-glial Circuits 1) Glial Cells Express mentioning

confidence: 99%

Astrocytes in Alzheimer's Disease

et al. 2010

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Summary:The circuitry of the human brain is formed by neuronal networks embedded into astroglial syncytia. The astrocytes perform numerous functions, providing for the overall brain homeostasis, assisting in neurogenesis, determining the micro-architecture of the grey matter, and defending the brain through evolutionary conserved astrogliosis programs.Astroglial cells are engaged in neurological diseases by determining the progression and outcome of neuropathological process. Astrocytes are specifically involved in various neurodegenerative diseases, including Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, and various forms of dementia. Recent evidence suggest that early stages of neurodegenerative processes are associated with atrophy of astroglia, which causes disruptions in synaptic connectivity, disbalance in neurotransmitter homeostasis, and neuronal death through increased excitotoxicity. At the later stages, astrocytes become activated and contribute to the neuroinflammatory component of neurodegeneration.

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“…They are located in the sarcoplasmic reticulum of skeletal muscle, where calcium release is important in muscle contraction, and also in the endoplasmic reticulum of neurons and other cell types, where they are heavily involved in calcium signalling (Sattelle et al, 2008). Each receptor is composed of a large cytoplasmic domain at the N terminus and a small transmembrane domain at the C terminus (Hamilton, 2005). Functional channels present as large homomeric tetramers.…”

Section: Ryanodine Receptorsmentioning

confidence: 99%

Identification of ion channel genes in the Acyrthosiphon pisum genome

Dale

Jones

Tamborindeguy

et al. 2010

Insect Molecular Biology

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Abstracti mb_975 141..154Aphids are major pests of crops, causing hundreds of millions of dollars worth of damage annually. Ion channel proteins are often the targets of modern insecticides and mutations in ion channel genes can lead to resistance to many leading classes of insecticides. The sequencing of the pea aphid, Acyrthosiphon pisum, genome has now allowed detailed in silico analysis of the aphid ion channels. The study has revealed significant differences in the composition of the ion channel families between the aphid and other insects. For example A. pisum does not appear to contain a homologue of the nACh receptor alpha 5 gene whilst the calcium channel beta subunit has been duplicated. These variations could result in differences in function or sensitivity to insecticides. The genome sequence will allow the study of aphid ion channels to be accelerated, leading to a better understanding of the function of these economically important channels. The potential for identifying novel insecticide targets within the aphid is now a step closer.

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Ryanodine receptors

Cited by 123 publications

References 88 publications

IP3 Receptors: Toward Understanding Their Activation

IP3 Receptors: Toward Understanding Their Activation

Astrocytes in Alzheimer's Disease

Identification of ion channel genes in the Acyrthosiphon pisum genome

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