Identification and characterization of PRG-1 as a neuronal calmodulin-binding protein

Tokumitsu, Hiroshi; Hatano, Naoya; Tsuchiya, Masaharu; Yurimoto, Saki; Fujimoto, Tomohito; Ohara, Naoki; Kobayashi, Ryōji; Sakagami, Hiroyuki

doi:10.1042/bj20100637

Cited by 32 publications

(35 citation statements)

References 45 publications

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“…PRG-1 is highly expressed in the forebrain and in the cerebellar cortex (30). It has been reported that overexpression of PRG-1 induces neurite outgrowth in PC12 cells (36) and that PRG-1 is up-regulated during periods of axonal outgrowth and attenuates LPA-induced axon collapse (27).…”

Section: Discussionmentioning

confidence: 99%

“…PRG-1 is an important molecule in the control of hippocampal excitability dependent on presynaptic LPA 2 receptor signaling (29). PRG-1 is likely to be a calmodulin (CaM)-interacting protein and is involved in postsynaptic functions regulated by intracellular Ca 2ϩ signaling (30). Deletion of Prg-1 in mice leads to epileptic seizures and augmentation of excitatory postsynaptic current (EPSC) but not inhibitory postsynaptic current (IPSC) (29).…”

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confidence: 99%

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TRIM67 Protein Negatively Regulates Ras Activity through Degradation of 80K-H and Induces Neuritogenesis

Yaguchi

Okumura

Takahashi

et al. 2012

Journal of Biological Chemistry

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Background: TRIM67, which is selectively expressed in the cerebellum, is a novel member of the TRIM protein family. Results: TRIM67 interacts with PRG-1 and 80K-H, which is involved in the Ras-mediated signaling pathway. Conclusion: TRIM67 regulates Ras signaling via degradation of 80K-H, leading to neural differentiation including neuritogenesis. Significance: Analysis of TRIM67 would provide therapeutic benefits for neurodegenerative diseases.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

TRIM67 Protein Negatively Regulates Ras Activity through Degradation of 80K-H and Induces Neuritogenesis

Yaguchi

Okumura

Takahashi

et al. 2012

Journal of Biological Chemistry

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“…Prg1 is a neuronal calmodulin‐binding protein that regulates intracellular calcium signaling (Tokumitsu et al, ). Calmodulin seems to be a key effector in calcium‐related cell survival (Gallo et al, ; Boutillier et al, ).…”

Section: Discussionmentioning

confidence: 99%

Plasticity‐related gene 1 is important for survival of neurons derived from rat neural stem cells

Hashimoto

Yamada

Iwai

et al. 2013

J of Neuroscience Research

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Plasticity-related gene 1 (Prg1) is a membrane-associated lipid phosphate phosphatase. In this study, we first investigated the role of Prg1 in the survival of neurons derived from rat neural stem cells (NSCs) using small interfering RNA (siRNA). Prg1 knock-down decreased the cell number. Interestingly, Prg1 knock-down increased genomic DNA fragmentation, suggesting the possible induction of apoptosis. Exogenously expressed Prg1 rescued the cells from death and restored the loss of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) activity induced with Prg1 siRNA. However, exogenously expressed mutated-Prg1 (the 253rd amino acid, histidine253, had been changed to alanine) did not rescue the cell death or restore the MTT activity. Histidine253 of Prg1 has been reported to be important for lipid phosphate phosphatase activity. These results suggest that Prg1 is important for survival of neurons through its dephosphorylation activity.

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“…Other Methods-The CaM overlay method was performed using 0.5 g/ml biotinylated CaM in the presence of 1 mM CaCl 2 , followed by detection of the CaM-binding signal using a chemiluminescence reagent (PerkinElmer Life Sciences) as described previously (28). Protein concentration was estimated by staining the samples with Coomassie Brilliant Blue (BioRad) using bovine serum albumin as a standard.…”

Section: Methodsmentioning

confidence: 99%

Differential AMP-activated Protein Kinase (AMPK) Recognition Mechanism of Ca2+/Calmodulin-dependent Protein Kinase Kinase Isoforms

Fujiwara

Kawaguchi

Fujimoto³

et al. 2016

Journal of Biological Chemistry

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Ca2؉ /calmodulin-dependent protein kinase kinase ␤ (CaMKK␤) is a known activating kinase for AMP-activated protein kinase (AMPK). In vitro, CaMKK␤ phosphorylates Thr 172 in the AMPK␣ subunit more efficiently than CaMKK␣, with a lower K m (ϳ2 M) for AMPK, whereas the CaMKI␣ phosphorylation efficiencies by both CaMKKs are indistinguishable. Here we found that subdomain VIII of CaMKK is involved in the discrimination of AMPK as a native substrate by measuring the activities of various CaMKK␣/CaMKK␤ chimera mutants. Sitedirected mutagenesis analysis revealed that Leu 358 in CaMKK␤/ Ile 322 in CaMKK␣ confer, at least in part, a distinct recognition of AMPK but not of CaMKI␣. Ca2ϩ /calmodulin-dependent protein kinase kinases (CaMKKs) 2 were originally identified as members of the calmodulin (CaM) kinase (CaMK) family that phosphorylate and activate two multifunctional CaMKs, including CaMKI and CaMKIV, constituting Ca 2ϩ -dependent kinase cascades named CaMK cascades (1-3). CaMKK in mammals is derived from two genes (CaMKK␣ and CaMKK␤), with ϳ70% of amino acid sequence homology in the catalytic domains (4 -6). The CaMKK/CaMKIV cascade has been shown to be involved in the regulation of gene expression through the phosphorylation of transcription factors such as cAMP-response element-binding protein (7,8) and serum response factor (9). In contrast, the CaMKK/CaMKI cascade plays an important role in neuronal development, including axon outgrowth (10), leptin-induced spine formation (11), and activity-dependent synaptogenesis (12). Except for the downstream CaMKs, AMP-activated protein kinase (AMPK) has been identified as a novel target kinase for CaMKK␤ (13-15), and the CaMKK␤/AMPK pathway has been demonstrated to be functional in various Ca 2ϩ -dependent AMPK-mediated signal transduction processes, including regulation of appetite and glucose homeostasis (16), stimulation of mitochondrial fatty acid oxidation by thyroid hormone T3 (17), and regulation of autophagy by amino acid starvation (18). According to studies using either RNA interference or pharmacological inhibition of CaMKK in HeLa cells, which do not express LKB1, an alternative AMPK kinase, CaMKK␤ has been shown to be responsible for Ca 2ϩ -dependent activation of AMPK in vivo, whereas both CaMKK isoforms are capable of phosphorylating the AMPK␣ subunit at Thr 172 in vitro (13-15). This was confirmed by the fact that STO-609 (19), a CaMKK inhibitor, suppressed ionomycin-induced AMPK phosphorylation in A549 cells (a human lung adenocarcinoma epithelial cell line) expressing STO-609-resistant CaMKK␣ but not . These results indicate that the CaMKK␤ isoform, rather than CaMKK␣, preferably recognizes AMPK, suggesting that the recognition mechanism of AMPK by CaMKK isoforms as a substrate may differ from that of CaMKI. A previous report showed that CaMKK␤, but not CaMKK␣, forms a stable complex with AMPK, which could explain why CaMKK␤ is an AMPK kinase and CaMKK␣ is not (21). However, Fogarty et al. (22) reported that CaMKK␤ activates AMPK without forming a stabl...

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Identification and characterization of PRG-1 as a neuronal calmodulin-binding protein

Cited by 32 publications

References 45 publications

TRIM67 Protein Negatively Regulates Ras Activity through Degradation of 80K-H and Induces Neuritogenesis

TRIM67 Protein Negatively Regulates Ras Activity through Degradation of 80K-H and Induces Neuritogenesis

Plasticity‐related gene 1 is important for survival of neurons derived from rat neural stem cells

Differential AMP-activated Protein Kinase (AMPK) Recognition Mechanism of Ca2+/Calmodulin-dependent Protein Kinase Kinase Isoforms

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