Characterizations of two forms of inositol 1,4,5-trisphosphate receptor in rat liver

Hilly, Mauricette; Claret, M; Mauger, Jean‐Pierre

doi:10.1016/0898-6568(90)90053-d

Cited by 37 publications

(38 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These subtypes of the IP 3 receptor are expressed to various degrees in different tissues (50), and more than one subtype may even be found localized to the same intracellular Ca 2ϩ pool (16). Heterogeneity of IP 3 receptors in both IP 3 binding and Ca 2ϩ releasing properties has also been suggested (54,55). Finally, cAMP-PK may act differently on different IP 3 receptor subtypes.…”

Section: Discussionmentioning

confidence: 99%

Inhibition of inositol 1,4,5-trisphosphate-induced Ca ²⁺ release by cAMP-dependent protein kinase in a living cell

Tertyshnikova

Fein

1998

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 99%

Inhibition of inositol 1,4,5-trisphosphate-induced Ca ²⁺ release by cAMP-dependent protein kinase in a living cell

Tertyshnikova

Fein

1998

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…An inhibition of the binding was observed in several (14,45,46) but not in all (47) studies. In hepatocytes Ca 2ϩ converts the InsP 3 R from a low affinity to a high affinity conformational state, thereby increasing the binding (10,48). Moreover, recent studies on InsP 3 Rs overexpressed in insect Sf9 cells demonstrate differences in Ca 2ϩ sensitivity of the InsP 3 binding between InsP 3 R isoforms 1 and 3 (49,50).…”

Section: ] Was Gradually Increased (Closed Circles) or Decreased (Opementioning

confidence: 99%

Molecular and Functional Evidence for Multiple Ca2+-binding Domains in the Type 1 Inositol 1,4,5-Trisphosphate Receptor

Sienaert

Missiaen

Smedt

et al. 1997

Journal of Biological Chemistry

138

104

View full text Add to dashboard Cite

Structural and functional analyses were used to investigate the regulation of the inositol 1,4,5-trisphosphate (InsP 3 ) receptor (InsP 3 R) by Ca 2؉ . To define the structural determinants for Ca 2؉ binding, cDNAs encoding GST fusion proteins that covered the complete linear cytosolic sequence of the InsP 3 R-1 were expressed in bacteria. The fusion proteins were screened for Ca 2؉ and ruthenium red binding through the use of 45 The inositol 1,4,5-trisphosphate receptor (InsP 3 R) 1 is an intracellular Ca 2ϩ release channel that is modulated by various physiological ligands such as inositol 1,4,5-trisphosphate (InsP 3 ), Ca 2ϩ , nucleotides, calmodulin (CaM), FK506BP, phosphatases, and kinases (reviewed in Refs. 1 and 2). The InsP 3 R can be divided into three functionally different domains as follows: an N-terminal ligand-binding domain, a modulatory domain, and a channel domain near the C terminus (3, 4). Among the various modulators, Ca 2ϩ itself plays a pivotal role and may be considered as a co-agonist exerting both positive and negative effects on InsP 3 -induced Ca 2ϩ release. Cytosolic Ca 2ϩ has a bell-shaped effect on the InsP 3 R, with low concentrations stimulating the release and high concentrations inhibiting the release (5-8). Both phases are time-dependent, but the inhibition develops more slowly than the stimulation (6, 9 -11). Although these kinetically distinct effects are believed to be crucial for the generation of Ca 2ϩ oscillations and waves (12), little is known about how Ca 2ϩ interacts with the InsP 3 R. Regulation might be exerted by direct binding of Ca 2ϩ to the InsP 3 R and/or via Ca 2ϩ -sensitive protein(s), e.g. via Ca 2ϩ /CaMdependent protein kinase II and protein phosphatase 2B (13) or via a Ca 2ϩ -sensitizing factor (14). Studies in which effects of Sr 2ϩ were compared with those of Ca 2ϩ revealed that at least two interaction sites must exist: a stimulatory site that is modestly sensitive to Sr 2ϩ and an inhibitory site that is nearly insensitive to Sr 2ϩ (15). One Ca 2ϩ -binding domain has been localized on the cytosolic side of the InsP 3 R-1 (16, 17), but whether this domain represents a stimulatory or an inhibitory interaction site is still unclear. Luminal Ca 2ϩ also regulates the InsP 3 -induced Ca 2ϩ release. Loading of the Ca 2ϩ stores results in a relatively more pronounced InsP 3 -induced Ca 2ϩ release (18 -21). A high affinity Ca 2ϩ -binding site was detected on the luminal loop (17), but its functional significance is not yet clear.The aim of the present work was two-fold. First, we wanted to investigate, at the structural level, the presence of direct Ca 2ϩ -binding sites on InsP 3 R-1. Second, we wanted to functionally demonstrate multiple Ca 2ϩ interactions on the InsP 3 R by a kinetic analysis of the effects of Ca 2ϩ and Sr 2ϩ on the InsP 3 -induced Ca 2ϩ release.For the first part of this study we constructed and expressed a number of GST fusion proteins that contain cytosolic fragments of the InsP 3 R sequence. The ability of these fusion proteins to bind ...

show abstract

“…The negative interaction between InsP $ and Ca# + described here might be specific to InsP $ R1. The effect of Ca# + on InsP $ binding to InsP $ R of type 2 [29,30] or type 3 [27,28] is different from that on InsP $ binding to the type 1 receptor. However, this does not exclude the possibility that the counteractive effect of InsP $ on the Ca# + -dependent inhibition of InsP $ R1 activity also occurs with other InsP $ R isoforms.…”

Section: [$H]inspmentioning

confidence: 81%

“…The molecular basis of the Ca# + -dependence might differ for each receptor. Ca# + inhibits InsP $ binding to InsP $ R1 [26][27][28][29] but it stimulates InsP $ binding to InsP $ R2 [29,30] and InsP $ R3 [27,28]. The inhibitory effect of InsP $ R1 has been reported to be mediated by calmedin, a membranous Ca# + -binding protein first detected in cerebellum, which is readily separated from InsP $ R [31].…”

Section: Introductionmentioning

confidence: 99%

Regulation of cerebellar Ins(1,4,5)P3 receptor by interaction between Ins(1,4,5)P3 and Ca2+

Coquil

Picard

Mauger

1999

Biochemical Journal

Self Cite

View full text Add to dashboard Cite

We have characterized in detail the Ca# + -dependent inhibition of [$H]Ins(1,4,5)P $ ([$H]InsP $ ) binding to sheep cerebellar microsomes, over a short duration (3 s), with the use of a perfusion protocol. This procedure prevented artifacts previously identified in studies of this Ca# + effect. In a cytosol-like medium at pH 7.1 and 20 mC, a maximal inhibition of approx. 50 % was measured. Both inhibition and its reversal were complete within 3 s. Ca# + decreased the affinity of the receptor for InsP $ by approx. 50 % (K d 146p24 nM at pCa 9 and 321p56 nM at pCa 5.3), without changing the total number of binding sites. Conversely, increasing the [$H]InsP $ concentration from 30 to 400 nM tripled the IC &! for Ca# + and decreased the maximal inhibition by 63 %. This is similar to a partial competitive inhibition between InsP $ binding and inhibitory Ca# + binding and is consistent with InsP $ and

show abstract

Characterizations of two forms of inositol 1,4,5-trisphosphate receptor in rat liver

Cited by 37 publications

References 30 publications

Inhibition of inositol 1,4,5-trisphosphate-induced Ca ²⁺ release by cAMP-dependent protein kinase in a living cell

Inhibition of inositol 1,4,5-trisphosphate-induced Ca ²⁺ release by cAMP-dependent protein kinase in a living cell

Molecular and Functional Evidence for Multiple Ca2+-binding Domains in the Type 1 Inositol 1,4,5-Trisphosphate Receptor

Regulation of cerebellar Ins(1,4,5)P3 receptor by interaction between Ins(1,4,5)P3 and Ca2+

Contact Info

Product

Resources

About

Characterizations of two forms of inositol 1,4,5-trisphosphate receptor in rat liver

Cited by 37 publications

References 30 publications

Inhibition of inositol 1,4,5-trisphosphate-induced Ca 2+ release by cAMP-dependent protein kinase in a living cell

Inhibition of inositol 1,4,5-trisphosphate-induced Ca 2+ release by cAMP-dependent protein kinase in a living cell

Molecular and Functional Evidence for Multiple Ca2+-binding Domains in the Type 1 Inositol 1,4,5-Trisphosphate Receptor

Regulation of cerebellar Ins(1,4,5)P3 receptor by interaction between Ins(1,4,5)P3 and Ca2+

Contact Info

Product

Resources

About

Inhibition of inositol 1,4,5-trisphosphate-induced Ca ²⁺ release by cAMP-dependent protein kinase in a living cell

Inhibition of inositol 1,4,5-trisphosphate-induced Ca ²⁺ release by cAMP-dependent protein kinase in a living cell