Calmodulin and Calmodulin-Binding Proteins in the Cell Nucleus

Bachs, Oriol; Carafoli, Ernesto

doi:10.1007/978-3-662-21686-6_5

Cited by 28 publications

(2 citation statements)

References 95 publications

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“…Ca2+ is important in nuclear function: nuclear vesicle fusion requires Ca2+ mobilization (28) and Ca2+ plays a role in the regulation of the immediate-early response genes (29). Additionally several kinases, some of them specific for the nucleus such as PKC-L and calmodulindependent kinase II, are targets for Ca2+-calmodulin signalling (30)(31)(32). Although the NPC is considered to be permeable to ions, differences between the [Ca2+] in the nucleoplasm and the cytosol have been observed.…”

Section: Ca2+ Transport Systems In the Nuclear Envelopementioning

confidence: 99%

Nuclear calcium and the regulation of the nuclear pore complex

1997

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In eukaryotic cells the nucleus and its contents are separated from the cytoplasm by the nuclear envelope. Macromolecules, as well as smaller molecules and ions, can cross the nuclear envelope through the nuclear pore complex. Molecules greater than approx. 60 kDa and containing a nuclear localization signal are actively transported across the nuclear membranes, but there has been little evidence for regulatory mechanisms for smaller molecules and ions. Recently, diffusion across the nuclear envelope has been observed to be regulated by nuclear cisternal Ca2+ concentrations. Following depletion of Ca2+ from the nuclear store by inositol 1,4,5-trisphosphate or Ca2+ chelators, a fluorescent 10 kDa marker molecule was no longer able to enter the nucleus. Distinct conformational states of the nuclear pore complexes depended on the Ca2+ filling state of the nuclear envelope, supporting the assumption that a switch in the conformation of the nuclear pore complex may control the transport of intermediate-sized molecules across the nuclear envelope. Thus nuclear Ca2+ stores may regulate the conformational state of the nuclear pore complex, and thereby passive diffusion of molecules between the cytosol and the nucleoplasm. The physiological significance of this finding is currently unknown.

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Section: Ca2+ Transport Systems In the Nuclear Envelopementioning

confidence: 99%

Nuclear calcium and the regulation of the nuclear pore complex

1997

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“…A variety of functions of protein is related to the ion binding: ion channels, ligand binding by a receptor, enzymatic reactions, and so on . For example, a calcium ion bound to calmodulin works as a coenzyme for controlling activity of other enzymes. , An ion works sometime as a “clamp” in the construction of protein to stabilize its conformation. Ion binding is quite essential in a variety of ion channels too.…”

Section: Introductionmentioning

confidence: 99%

Selective Ion Binding by Protein Probed with the Statistical Mechanical Integral Equation Theory

2007

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Selective ion binding by human lysozyme and its mutants is probed with the three-dimensional interaction site model theory which is the statistical mechanical integral equation theory. Preliminary and partial results of the study have been already published (Yoshida, N. et al. J. Am. Chem. Soc. 2006, 128, 12042-12043). The calculation was carried out for aqueous solutions of three different electrolytes, CaCl2, NaCl, and KCl, and for four different mutants of the human lysozyme: wild type, Q86D, A92D, and Q86D/A92D, which have been studied experimentally. The discussion of this article focuses on the cleft that consists of amino acid residues from Q86 to A92. For the wild type of protein in the aqueous solutions of all the electrolytes studied, there are no distributions observed for the ions inside the cleft. The Q86D mutant shows essentially the same behavior with that of the wild type. The A92D mutant shows strong binding ability to Na+ in the recognition site, which is in accord with the experimental results. There are two isomers of the Q86D/A92D mutant, e.g., apo-Q86D/A92D and holo-Q86D/A92D. Although both isomers exhibit the binding ability to the Na+ and Ca2+ ions, the holo isomer shows much greater affinity compared with the apo isomer. Regarding the selective ion binding of the holo-Q86D/A92D mutant, it shows greater affinity to Ca2+ than to Na+, which is also consistent with the experimental observation.

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Most calbindin‐immunoreactive neurons, but few calretinin‐immunoreactive neurons, express the m1 acetylcholine receptor in the middle temporal visual area of the macaque monkey

Coppola

Disney

2018

Brain and Behavior

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IntroductionRelease of the neuromodulator acetylcholine into cortical circuits supports cognition, although its precise role and mechanisms of action are not well understood. Little is known about functional differences in cholinergic modulatory effects across cortical model systems, but anatomical evidence suggests that such differences likely exist because, for example, the expression of cholinergic receptors differs profoundly both within and between species.MethodsIn the primary visual cortex (V1) of macaque monkeys, cholinergic receptors are strongly expressed by inhibitory interneurons. Using dual‐immunofluorescence confocal microscopy, we examine m1 muscarinic acetylcholine receptor expression by two subclasses of inhibitory interneurons—identified by their expression of the calcium‐binding proteins calbindin and calretinin—in the middle temporal extrastriate area (MT) of the macaque.Results and ConclusionsWe find that the majority of calbindin‐immunoreactive neurons (55%) and only few calretinin‐immunoreactive neurons (10%) express the m1 acetylcholine receptor. These results differ from the pattern observed in V1 of the same species, lending further support to the notion that cholinergic modulation in the cortex is tuned such that different cortical compartments will respond to acetylcholine release in different ways.

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Calmodulin and Calmodulin-Binding Proteins in the Cell Nucleus

Cited by 28 publications

References 95 publications

Nuclear calcium and the regulation of the nuclear pore complex

Nuclear calcium and the regulation of the nuclear pore complex

Selective Ion Binding by Protein Probed with the Statistical Mechanical Integral Equation Theory

Most calbindin‐immunoreactive neurons, but few calretinin‐immunoreactive neurons, express the m1 acetylcholine receptor in the middle temporal visual area of the macaque monkey

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