Calcium dependent phosphodiesterase activity and its activating factor (PAF) from brain

Kakiuchi, Shiro; Yamazaki, Reiko

doi:10.1016/0006-291x(70)90199-3

Cited by 487 publications

(118 citation statements)

References 4 publications

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“…In 1970, CaM was first discovered to activate cyclic nucleotide phosphodiesterase (17,18). Subsequently, many proteins such as Ca 2ϩ -transporting ATPase (102,103), myosin light chain kinase (8) and phosphorylase kinase (10) were all found to be regulated by CaM.…”

Section: Conformational Plasticity In Calmodulinmentioning

confidence: 99%

Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: Two ways to promote multifunctionality

Ikura

Ames

2006

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

239

202

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Calcium signaling pathways control a variety of cellular events such as gene transcription, protein phosphorylation, nucleotide metabolism, and ion transport. These pathways often involve a large number of calcium-binding proteins collectively known as the calmodulin or EF-hand protein superfamily. Many EF-hand proteins undergo a large conformational change upon binding to Ca 2؉ and target proteins. All members of the superfamily share marked sequence homology and similar structural features required to sense Ca 2؉ . Despite such structural similarities, the functional diversity of EF-hand calcium-binding proteins is extraordinary. Calmodulin itself can bind >300 different proteins, and the many members of the neuronal calcium sensor and S100 protein families collectively recognize a largely different set of target proteins. Recent biochemical and structural studies of many different EF-hand proteins highlight remarkable similarities and variations in conformational responses to the common ligand Ca 2؉ and their respective cellular targets. In this review, we examine the essence of molecular recognition activities and the mechanisms by which calmodulin superfamily proteins control a wide variety of Ca 2؉ signaling processes.

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Section: Conformational Plasticity In Calmodulinmentioning

confidence: 99%

Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: Two ways to promote multifunctionality

Ikura

Ames

2006

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

239

202

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“…Calcium's role in neurotransmitter release from the presynaptic nerve terminal has been of great interest, yet little is known about the molecular mechanisms of Ca2+ in stimulating neurotransmitter release or its other physiological functions in the nerve terminal (1). Recent studies have suggested that some of calcium's effects on nerve function may be modulated by a heat-stable Ca2+-dependent regulator protein (calmodulin), since the Ca2+-dependent activation of several important enzyme systems in brain required calmodulin (2)(3)(4)(5). Calmodulin has been purified and characterized from many sources and appears to be a Ca2+ receptor protein with a specific and strong binding affinity for Ca2+ (6)(7)(8).…”

mentioning

confidence: 99%

Stimulation of Ca ²⁺ -dependent neurotransmitter release and presynaptic nerve terminal protein phosphorylation by calmodulin and a calmodulin-like protein isolated from synaptic vesicles

DeLorenzo

Freedman

Yohe

et al. 1979

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

295

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Synaptic vesicles have a Ca2+-dependent protein kinase system that may play a role in mediating Ca2+-stimulated neurotransmitter release and vesicle function. Calcium's ability to initiate norepinephrine release and protein phosphorylation in synaptic vesicle preparations was shown to be stimulated by the presence of an endogenous heat-stable vesicle protein fraction. The heat stability and characteristics of this endogenous vesicle fraction were similar to those of calmodulin (Ca2+-dependent regular protein) isolated from rat and bovine brain. Calmodulin, like endogenous heat-stable vesicle factor, restored calcium's ability to stimulate vesicle neurotransmitter release and protein kinase activity. Calmodulin-like vesicle protein and purified calmodulin were also equally effective in stimulating cyclic nucleotide-dependent phosphodiesterase, further indicating that these two proteins are functionally equivalent. Depolarization-dependent Ca2+ uptake in intact synaptosomes simultaneously stimulated release of neurotransmitter and phosphorylation of particular synaptic vesicle proteins that were shown in the isolated vesicle preparation to be dependent on Ca2+ and calmodulin. The results suggest that calcium's effects on neurotransmitter release and presynaptic nerve terminal protein phosphorylation may be mediated by endogenous calmodulin-like proteins.

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“…One aspect that we did not explore is whether Ca 2ϩ signaling could modulate the net effect of PDE1/PDE2 interplay on AMPAR trafficking. This is especially pertinent, as PDE1 is a Ca 2ϩ /calmodulinactivated PDE (57)(58)(59), and this regulatory feature could potentially disrupt PDE2 cross-activation and affect AMPAR trafficking dynamics. We speculate that, under high Ca 2ϩ conditions, PDE1 is fully activated, reducing the cGMP pool that controls PDE2 activity and resulting in a less active form of PDE2 and perhaps modulating surface GluA1 expression.…”

Section: Discussionmentioning

confidence: 99%

Cross-regulation of Phosphodiesterase 1 and Phosphodiesterase 2 Activities Controls Dopamine-mediated Striatal α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptor Trafficking

Song¹,

Tolentino

Sobie

et al. 2016

Journal of Biological Chemistry

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Dopamine, a key striatal neuromodulator, increases synaptic strength by promoting surface insertion and/or retention of AMPA receptors (AMPARs). This process is mediated by the phosphorylation of the GluA1 subunit of AMPAR by cyclic nucleotide-dependent kinases, making cyclic nucleotide phosphodiesterases (PDEs) potential regulators of synaptic strength. In this study, we examined the role of phosphodiesterase 2 (PDE2), a medium spiny neuron-enriched and cGMP-activated PDE, in AMPAR trafficking. We found that inhibiting PDE2 resulted in enhancement of dopamine-induced surface GluA1 expression in dopamine receptor 1-expressing medium spiny neurons. Using pharmacological and genetic approaches, we found that inhibition of PDE1 resulted in a decrease in surface AMPAR levels because of the allosteric activation of PDE2. The cross-regulation of PDE1 and PDE2 activities results in counterintuitive control of surface AMPAR expression, making it possible to regulate the directionality and magnitude of AMPAR trafficking.

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Calcium dependent phosphodiesterase activity and its activating factor (PAF) from brain

Cited by 487 publications

References 4 publications

Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: Two ways to promote multifunctionality

Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: Two ways to promote multifunctionality

Stimulation of Ca ²⁺ -dependent neurotransmitter release and presynaptic nerve terminal protein phosphorylation by calmodulin and a calmodulin-like protein isolated from synaptic vesicles

Cross-regulation of Phosphodiesterase 1 and Phosphodiesterase 2 Activities Controls Dopamine-mediated Striatal α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptor Trafficking

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Calcium dependent phosphodiesterase activity and its activating factor (PAF) from brain

Cited by 487 publications

References 4 publications

Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: Two ways to promote multifunctionality

Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: Two ways to promote multifunctionality

Stimulation of Ca 2+ -dependent neurotransmitter release and presynaptic nerve terminal protein phosphorylation by calmodulin and a calmodulin-like protein isolated from synaptic vesicles

Cross-regulation of Phosphodiesterase 1 and Phosphodiesterase 2 Activities Controls Dopamine-mediated Striatal α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptor Trafficking

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Stimulation of Ca ²⁺ -dependent neurotransmitter release and presynaptic nerve terminal protein phosphorylation by calmodulin and a calmodulin-like protein isolated from synaptic vesicles