Structure and expression of the rat inositol 1,4,5-trisphosphate receptor.

Mignery, Gregory A.; Newton, C L; Archer, Branch T.; Südhof, Thomas C.

doi:10.1016/s0021-9258(19)38397-8

Cited by 459 publications

(77 citation statements)

References 50 publications

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“…The Dogma: IP 3 R2 the Sole Functional Astrocytic IP 3 R There are three mammalian IP 3 R subtypes, i.e., IP 3 R1 (Furuichi et al, 1989;Mignery et al, 1989;Yamada et al, 1994), IP 3 R2 (Mignery et al, 1990;Südhof et al, 1991;Yamamoto-Hino et al, 1994;Iwai et al, 2005), and IP 3 R3 (Blondel et al, 1993;Yamamoto-Hino et al, 1994;Iwai et al, 2005). Among them, IP 3 R2 has widely been accepted as the only functional IP 3 R subtype present in astrocytes, and consequently, the IP 3 R2KO model mouse has been at the center of numerous important studies (Agulhon et al, 2010;Takata et al, 2011;Chen et al, 2012;Navarrete et al, 2012Navarrete et al, , 2019Cao et al, 2013;Perez-Alvarez et al, 2014;Petravicz et al, 2014;Gómez-Gonzalo et al, 2015Mariotti et al, 2016;Monai et al, 2016;Perea et al, 2016;Martin-Fernandez et al, 2017;Tanaka et al, 2017).…”

Section: Evidence For Three Subtypesmentioning

confidence: 99%

Astrocytic IP3Rs: Beyond IP3R2

Sherwood

Arizono

Panatier

et al. 2021

Front. Cell. Neurosci.

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Astrocytes are sensitive to ongoing neuronal/network activities and, accordingly, regulate neuronal functions (synaptic transmission, synaptic plasticity, behavior, etc.) by the context-dependent release of several gliotransmitters (e.g., glutamate, glycine, D-serine, ATP). To sense diverse input, astrocytes express a plethora of G-protein coupled receptors, which couple, via Gi/o and Gq, to the intracellular Ca2+ release channel IP3-receptor (IP3R). Indeed, manipulating astrocytic IP3R-Ca2+ signaling is highly consequential at the network and behavioral level: Depleting IP3R subtype 2 (IP3R2) results in reduced GPCR-Ca2+ signaling and impaired synaptic plasticity; enhancing IP3R-Ca2+ signaling affects cognitive functions such as learning and memory, sleep, and mood. However, as a result of discrepancies in the literature, the role of GPCR-IP3R-Ca2+ signaling, especially under physiological conditions, remains inconclusive. One primary reason for this could be that IP3R2 has been used to represent all astrocytic IP3Rs, including IP3R1 and IP3R3. Indeed, IP3R1 and IP3R3 are unique Ca2+ channels in their own right; they have unique biophysical properties, often display distinct distribution, and are differentially regulated. As a result, they mediate different physiological roles to IP3R2. Thus, these additional channels promise to enrich the diversity of spatiotemporal Ca2+ dynamics and provide unique opportunities for integrating neuronal input and modulating astrocyte–neuron communication. The current review weighs evidence supporting the existence of multiple astrocytic-IP3R isoforms, summarizes distinct sub-type specific properties that shape spatiotemporal Ca2+ dynamics. We also discuss existing experimental tools and future refinements to better recapitulate the endogenous activities of each IP3R isoform.

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Section: Evidence For Three Subtypesmentioning

confidence: 99%

Astrocytic IP3Rs: Beyond IP3R2

Sherwood

Arizono

Panatier

et al. 2021

Front. Cell. Neurosci.

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“…Molecular cloning reveals three different isoforms encoded by different genes, IP 3 R1, 2, and 3 (Furuichi et al, 1989;Mignery et al, 1989;Sudhof et al, 1991;Ross et al, 1992;Blondel et al, 1993;Maranto, 1994;De Smedt et al, 1997). Regulation of IP 3 receptors is complex with alternative splicing of at least IP 3 R1 (Mignery et al, 1990;Nakagawa et al, 1991;Danoff et al, 1991;Schell et. al., 1993;Nucifora et al, 1995) and posttranslational modification of IP 3 R by phosphorylation (Danoff et al, 1991;Ferris et al, 1991;Furuichi et al, 1994).…”

mentioning

confidence: 99%

Differential cellular expression of isoforms of inositol 1,4,5-triphosphate receptors in neurons and glia in brain

Sharp

Nucifora

Blondel³

et al. 1999

J. Comp. Neurol.

186

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Inositol 1,4,5-trisphosphate receptors (IP 3 R) are mediators of second messenger-induced intracellular calcium release. Three isoforms are known to be expressed in brain, but their regional distributions and cellular localizations are little known. In order to better understand the roles of IP 3 receptor isoforms in brain function, a first step is to define their distributions. We have used affinity-purified antibodies directed against peptides unique to each isoform to determine their sites of expression in rat brain. Type 1 IP 3 R (IP 3 R1) is dramatically enriched in Purkinje neurons in cerebellum and neurons in other regions, consistent with previous studies. By contrast, IP 3 R2 is only detected in glia, whereas IP 3 R3 is predominantly neuronal, with little detected in glia. IP 3 R3 is enriched in neuropil, especially in neuronal terminals (which often contain large dense core vesicles) in limbic and basal forebrain regions including olfactory tubercle, central nucleus of the amygdala, and bed nucleus of the stria terminalis. In addition, IP 3 R1 and IP 3 R3 have clearly distinct time courses of expression in developing brains. These data suggest separate roles for inositol 1,4,5trisphosphate receptor isoforms in development, and for glial and neuronal function. The IP 3 R3 may be involved in regulation of neurotransmitter or neuropeptide release in terminals within specific nuclei of the basal forebrain and limbic system.

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“…We first aimed to determine the partial nucleotide sequences flanking the S1 and S2 splicing segments of cDNA for porcine type 1 InsP $ receptor. All the primers were synthesized on the basis of the rat cDNA sequence reported by Mignery et al [3] with degenerative nucleotides introduced at the 3h-end portion of each primer. The primers used for amplification of the sequences flanking the S1 splicing segment were : IPR1-1, 5h-TTCCATGCTGA(A\G)CA(A\G)GA(A\G)AA(A\G)TT-3h (bases 1056-1078) ; IPR1-2, 5h-CGTTCCACCCGT(A\G\C\ T)AC(A\G)AA(A\G)TA(A\G\C\T)AC-3h (bases 1770-1793).…”

Section: Reverse Transcriptase-pcr Analysismentioning

confidence: 99%

“…The primers used for amplification of sequences flanking the S2 splicing segment were : IPR2-1, 5h-GACATCGTGTCTGCCCT-(A\G\C\T)GA(A\G)GA-3h (bases 5145-5167) ; IPR2-2, 5h-CGATCGTAAAAGACCTT(A\G)AA(A\G)AA-3h (bases 5892-5914). Nucleotide numbering was based on that of the rat cDNA sequence [3]. Each reaction mixture contained 50 mM KCl, 10 mM Tris\HCl, pH 8.3, 1.5 mM MgCl # , 0.001 % (w\v) gelatin, 0.2 mM each of dNTPs, 1 µM each of primers, 25 units\ml of Taq DNA polymerase (Perkin-Elmer\Cetus), and 4 % (v\v) first-strand cDNA products of poly(A) + RNA from porcine cerebellum.…”

Section: Reverse Transcriptase-pcr Analysismentioning

confidence: 99%

“…The release is initiated through binding of the compound to a specific receptor composed of four subunits constituting an InsP $ -gated Ca# + channel and localized to the endo\sarcoplasmic reticulum. Recent molecular cloning studies revealed the existence of at least four types of InsP $ receptor subunit encoded by different genes designated as 1 [2,3], 2 [4], 3 [5] and 4 [6]. The cerebellar receptor belongs to type 1, but is further diversified by alternative splicing [7,8].…”

Section: Introductionmentioning

confidence: 99%

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Isolation and characterization of vascular smooth muscle inositol 1,4,5-trisphosphate receptor

Islam

Yoshida

Koga

et al. 1996

Biochemical Journal

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myo-Inositol 1,4,5-trisphosphate (InsP3) receptor of porcine aorta was purified to near homogeneity and its biochemical properties were compared with those of cerebellar InsP3 receptor of the same animal species. The aortic InsP3 receptor consisted of equal amounts of two polypeptides with slightly differing molecular masses of around 240 kDa and was found to possess a single population of InsP3-binding site (Kd of 1.2 nM). The InsP3 receptor purified from porcine cerebellum was also comprised of two polypeptides. However, the molecular mass was slightly but definitely larger, being 250 kDa, and the amounts of the two polypeptides were not equal. The aortic InsP3 receptor cross-reacted with polyclonal antibody specific to type 1 InsP3 receptor as did the cerebellar InsP3 receptor. The aortic InsP3 receptor bound to calmodulin-Sepharose in a Ca(2+)-dependent manner, while the cerebellar InsP3 receptor did not. Reverse transcriptase-PCR analysis revealed two splicing variants of the type 1 InsP3 receptor in porcine aortic smooth muscle distinct from those of the type 1 InsP3 receptor of porcine cerebellum. The possible relevance of this difference to difference in calmodulin-binding property was discussed.

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Structure and expression of the rat inositol 1,4,5-trisphosphate receptor.

Cited by 459 publications

References 50 publications

Astrocytic IP3Rs: Beyond IP3R2

Astrocytic IP3Rs: Beyond IP3R2

Differential cellular expression of isoforms of inositol 1,4,5-triphosphate receptors in neurons and glia in brain

Isolation and characterization of vascular smooth muscle inositol 1,4,5-trisphosphate receptor

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