Ca2+ Signaling and Intracellular Ca2+ Binding Proteins

Niki, Ichiro; Yokokura, Hisayuki; Sudo, Toshiki; Kato, Masumi; Hidaka, Hiroyoshi

doi:10.1093/oxfordjournals.jbchem.a021466

Cited by 122 publications

(77 citation statements)

References 115 publications

(130 reference statements)

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“…On the basis of the primary structures responsible for the actual binding of these domains, intracellular Ca 2ϩ -binding proteins can be classified in the following three categories: EF-hand proteins, Ca 2ϩ /phospholipid-binding proteins (annexins and C2 region proteins), and Ca 2ϩ storage proteins (e.g. calsequestrin, calreticulin) (53). We have compared the typical sequence motifs of these three categories of Ca 2ϩ -binding proteins with the Ca 2ϩ -binding regions that we have detected in the InsP 3 R. None of the regions showed resemblance with known motifs.…”

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

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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 ...

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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

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“…Many calcium-mediated effects have been well characterized in other systems (Carafoli, 1987;Heizman and Hunziker, 1991;Ikura, 1996;Niki et al, 1996). In these cases, the physiological effects of calcium are often mediated indirectly by signal proteins.…”

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“…By binding calcium, these proteins undergo conformational changes that enable interaction with and modulation of effector proteins that cause the physiological changes linked to the calcium stimulus. Many of these calcium-signal proteins are well characterized and have been subgrouped based on structural and biochemical features (Heizman and Hunziker, 1991;Nakayama and Kretsinger, 1994;Niki et al, 1996). The majority are intracellular constituents, but some members may be secreted and have intercellular actions (Zimmer et al, 1995).…”

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confidence: 99%

“…The majority are intracellular constituents, but some members may be secreted and have intercellular actions (Zimmer et al, 1995). Several target proteins for these calcium-binding proteins have been identified, enabling biochemical definition of many of the physiological effects associated with calcium (Nakayama and Kretsinger, 1994;Zimmer et al, 1995;Niki et al, 1996).…”

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Characterization and Immunolocalization of a Cytosolic Calcium-Binding Protein from Brassica napus and Arabidopsis Pollen1

Rozwadowski

Zhao

Jackman³

et al. 1999

Plant Physiology

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Two low-molecular-weight proteins have been purified from Brassica napus pollen and a gene corresponding to one of them has been isolated. The gene encodes an 8.6-kD protein with two EFhand calcium-binding motifs and is a member of a small gene family in B. napus. The protein is part of a family of pollen allergens recently identified in several evolutionarily distant dicot and monocot plants. Homologs have been detected in Arabidopsis, from which one gene has been cloned in this study, and in snapdragon (Antirrhinum majus), but not in tobacco (Nicotiana tabacum). Expression of the gene in B. napus was limited to male tissues and occurred during the pollen-maturation phase of anther development. Both the B. napus and Arabidopsis proteins interact with calcium, and the potential for a calcium-dependent conformational change was demonstrated. Given this affinity for calcium, the cloned genes were termed BPC1 and APC1 (B. napus and Arabidopsis pollen calcium-binding protein 1, respectively). Immunolocalization studies demonstrated that BPC1 is found in the cytosol of mature pollen. However, upon pollen hydration and germination, there is some apparent leakage of the protein to the pollen wall. BPC1 is also concentrated on or near the surface of the elongating pollen tube. The essential nature of calcium in pollen physiology, combined with the properties of BPC1 and its high evolutionary conservation suggests that this protein plays an important role in pollination by functioning as a calcium-sensitive signal molecule.

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“…Intracellular calcium ions (Ca 2+ ) is very important in morphogenesis (Niki et al, 1996; Berridge, (Tsuruwaka et al, 2007(Tsuruwaka et al, & 2016. We also reported that morphological changes brought about 35 dramatic transition in Ca 2+ signaling (Tsuruwaka, Konishi & Shimada, 2015 …”

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Ca2+ Signaling and Intracellular Ca2+ Binding Proteins

Cited by 122 publications

References 115 publications

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

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

Characterization and Immunolocalization of a Cytosolic Calcium-Binding Protein from Brassica napus and Arabidopsis Pollen1

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