Phosphorylation and Up-regulation of Diacylglycerol Kinase γ via Its Interaction with Protein Kinase Cγ

Yamaguchi, Yasushi; Shirai, Yasuhito; Matsubara, Takehiro; Sanse, Koichi; Kuriyama, Masami; Oshiro, Noriko; Yoshino, Ken‐ichi; Yonezawa, Kazuyoshi; Ono, Yoshitaka; Saito, Naoaki

doi:10.1016/s0021-9258(19)84076-0

Cited by 21 publications

(17 citation statements)

References 46 publications

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“…The signaling characteristics were determined by measuring the M/C ratio of both DAG effector molecules, that is, PKCγ and DGKγ, and temporal dynamics of Ca 2+ and DAG. The results reported here are based on slower kinetics in CHO cells (Figure 4) and faster kinetics in PCs (Figure 5) (Yamaguchi et al, 2006;Adachi et al, 2008;Shuvaev et al, 2011). Membrane-to-cytosol (M/C) translocation characteristics of both DAG effector molecules, that is, PKCγ and DGKγ, are a key component of this subsignaling loop.…”

Section: Signaling Characteristics Of the Trpc3-mediated Signalosome ...mentioning

confidence: 86%

“…This work explores how the TRPC3-mediated local signalosome may regulate the gating characteristics of TRPC3 channels in PCs and CHO cells. The following experimental observations may provide some rationality for this investigation: (1) In CHO cells, ATP-induced purinergic receptor activation leads to DAG generation at the membrane, which in turn induces a local functional coupling between its effector molecules, thus ultimately restoring the DAG and Ca 2+ homeostasis ( Yamaguchi et al, 2006 ; Adachi et al, 2008 ). (2) In PCs, mutant PKCγ is constitutively active, whereas wild-type PKCγ is inactive, during basal conditions ( Shuvaev et al, 2011 ; Wong et al, 2018 ).…”

Section: Introductionmentioning

confidence: 99%

“…(6) In PCs, the WT PKCγ quickly translocates to the membrane on a KCl-modulated membrane-depolarization event and has a membrane residence time of 18 s ( Shuvaev et al, 2011 ). (7) TRPC3 activation allows Ca 2+ flux in CHO cells and PCs ( Yamaguchi et al, 2006 ; Adachi et al, 2008 ; Shuvaev et al, 2011 ). (8) The Ca 2+ influx is responsible for PKCγ and DGKγ translocation to the membrane in CHO cells ( Yamaguchi et al, 2006 ; Adachi et al, 2008 ).…”

Section: Introductionmentioning

confidence: 99%

“…(7) TRPC3 activation allows Ca 2+ flux in CHO cells and PCs ( Yamaguchi et al, 2006 ; Adachi et al, 2008 ; Shuvaev et al, 2011 ). (8) The Ca 2+ influx is responsible for PKCγ and DGKγ translocation to the membrane in CHO cells ( Yamaguchi et al, 2006 ; Adachi et al, 2008 ). (9) Evidence suggests that TRPC3 signals are downstream of mGluR1 ( Hartmann et al, 2008 ).…”

Section: Introductionmentioning

confidence: 99%

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TRPC3 Channel Activity and Viability of Purkinje Neurons can be Regulated by a Local Signalosome

Aslam¹,

Alvi

2022

Front. Mol. Biosci.

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Canonical transient receptor potential channels (TRPC3) may play a pivotal role in the development and viability of dendritic arbor in Purkinje neurons. This is a novel postsynaptic channel for glutamatergic synaptic transmission. In the cerebellum, TRPC3 appears to regulate functions relating to motor coordination in a highly specific manner. Gain of TRPC3 function is linked to significant alterations in the density and connectivity of dendritic arbor in Purkinje neurons. TRPC3 signals downstream of class I metabotropic glutamate receptors (mGluR1). Moreover, diacylglycerol (DAG) can directly bind and activate TRPC3 molecules. Here, we investigate a key question: How can the activity of the TRPC3 channel be regulated in Purkinje neurons? We also explore how mGluR1 activation, Ca2+ influx, and DAG homeostasis in Purkinje neurons can be linked to TRPC3 activity modulation. Through systems biology approach, we show that TRPC3 activity can be modulated by a Purkinje cell (PC)–specific local signalosome. The assembly of this signalosome is coordinated by DAG generation after mGluR1 activation. Our results also suggest that purinergic receptor activation leads to the spatial and temporal organization of the TRPC3 signaling module and integration of its key effector molecules such as DAG, PKCγ, DGKγ, and Ca2+ into an organized local signalosome. This signaling machine can regulate the TRPC3 cycling between active, inactive, and desensitized states. Precise activity of the TRPC3 channel is essential for tightly regulating the Ca2+ entry into PCs and thus the balance of lipid and Ca2+ signaling in Purkinje neurons and hence their viability. Cell-type–specific understanding of mechanisms regulating TRPC3 channel activity could be key in identifying therapeutic targeting opportunities.

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Section: Signaling Characteristics Of the Trpc3-mediated Signalosome ...mentioning

confidence: 86%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

TRPC3 Channel Activity and Viability of Purkinje Neurons can be Regulated by a Local Signalosome

Aslam¹,

Alvi

2022

Front. Mol. Biosci.

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“…This may be due to the rapid metabolism of DG by endogenous DG kinase (DGK) (Topham and Prescott 1999), whereas TPA cannot be metabolized by the same enzymes. In fact, DGK inhibitor delayed the retranslocation of γPKC–GFP from the plasma membrane to the cytoplasm (Shirai et al 2000b; Yamaguchi et al 2006).…”

Section: Discussionmentioning

confidence: 99%

Immunogold Electron Microscopic Demonstration of Distinct Submembranous Localization of the Activated γPKC Depending on the Stimulation

Oyasu

Fujimiya

Kashiwagi

et al. 2007

J Histochem Cytochem.

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We examined the precise intracellular translocation of gamma subtype of protein kinase C (gammaPKC) after various extracellular stimuli using confocal laser-scanning fluorescent microscopy (CLSM) and immunogold electron microscopy. By CLSM, treatment with 12-O-tetradecanoylphorbol-13-acetate (TPA) resulted in a slow and irreversible accumulation of green fluorescent protein (GFP)-tagged gammaPKC (gammaPKC-GFP) on the plasma membrane. In contrast, treatment with Ca(2+) ionophore and activation of purinergic or NMDA receptors induced a rapid and transient membrane translocation of gammaPKC-GFP. Although each stimulus resulted in PKC localization at the plasma membrane, electron microscopy revealed that gammaPKC showed a subtle but significantly different localization depending on stimulation. Whereas TPA and UTP induced a sustained localization of gammaPKC-GFP on the plasma membrane, Ca(2+) ionophore and NMDA rapidly translocated gammaPKC-GFP to the plasma membrane and then restricted gammaPKC-GFP in submembranous area (<500 nm from the plasma membrane). These results suggest that Ca(2+) influx alone induced the association of gammaPKC with the plasma membrane for only a moment and then located this enzyme at a proper distance in a touch-and-go manner, whereas diacylglycerol or TPA tightly anchored this enzyme on the plasma membrane. The distinct subcellular targeting of gammaPKC in response to various stimuli suggests a novel mechanism for PKC activation.

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Both the C1 domain and a basic amino acid cluster at the C-terminus are important for the neurite and branch induction ability of DGKβ

Kano¹,

Kouzuki²,

Mizuno³

et al. 2014

Biochemical and Biophysical Research Communications

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Phosphorylation and Up-regulation of Diacylglycerol Kinase γ via Its Interaction with Protein Kinase Cγ

Cited by 21 publications

References 46 publications

TRPC3 Channel Activity and Viability of Purkinje Neurons can be Regulated by a Local Signalosome

TRPC3 Channel Activity and Viability of Purkinje Neurons can be Regulated by a Local Signalosome

Immunogold Electron Microscopic Demonstration of Distinct Submembranous Localization of the Activated γPKC Depending on the Stimulation

Both the C1 domain and a basic amino acid cluster at the C-terminus are important for the neurite and branch induction ability of DGKβ

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