Protein Phosphatase 2A Is Associated with Class C L-type Calcium Channels (Cav1.2) and Antagonizes Channel Phosphorylation by cAMP-dependent Protein Kinase

Davare, Monika A.; Horne, Mary C.; Hell, Johannes

doi:10.1074/jbc.m005462200

Cited by 165 publications

(177 citation statements)

References 68 publications

(57 reference statements)

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“…PP2a is also activated by p38 MAPK in the brain, where it can modulate serotonin transporters (Zhu et al, 2005). PP2a binds to the C terminus of ␣-1C calcium channels, and reverses PKA (protein kinase A) -mediated phosphorylation of serine 1928 located inside this C-terminal region (Davare et al, 2000). A recent report has also demonstrated direct interaction of the protein phosphatase 2C␣ (PP2C␣) to the C terminus of both N-and P/Q-type calcium channels, and that PP2C␣ reverses phosphorylation of these neuronal calcium channels by PKC (protein kinase C) (Li et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

p38 Mitogen-Activated Protein Kinase Contributes to Adenosine A₁Receptor-Mediated Synaptic Depression in Area CA1 of the Rat Hippocampus

Brust

Cayabyab²,

Zhou³

et al. 2006

J. Neurosci.

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Section: Discussionmentioning

confidence: 99%

p38 Mitogen-Activated Protein Kinase Contributes to Adenosine A₁Receptor-Mediated Synaptic Depression in Area CA1 of the Rat Hippocampus

Brust

Cayabyab²,

Zhou³

et al. 2006

J. Neurosci.

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“…Interestingly, ␣4 does not associate with the core enzyme, suggesting that ␣4 competes with the A subunit for binding to C␣. Other examples of C␣ subunit binding partners are the class C L-type calcium channel (25), the homeobox protein HOX11 (26), and the translation termination factor eRF1 (27). The latter case is of particular interest because it was demonstrated that the eRF1 binding domain is located within the N-terminal 50 amino acids of C␣.…”

Section: Discussionmentioning

confidence: 99%

“…As a control, a mock purification was carried out in parallel using lysate from cells transfected with empty vector pcDNA3. In panel a, the exposure times are 20 min for A␣ EE (lanes 1-21), 16 h for A␣ EE (lanes [22][23][24][25][26][27][28], and 5 min for the Bs and Cs. In panel b, the exposure times are 30 s for A␤ EE (lanes 1-10), 20 min for A␤ EE (lanes [11][12][13][14][15][16][17][18][19][20], 5 min for the Bs and Cs (lanes 1-5), and 30 min for the Bs and Cs (lanes 6 -20).…”

Section: Three-step Purification Of A␣-c␣-bљ/pr72 Holoenzyme Usingmentioning

confidence: 99%

The Formation and Activity of PP2A Holoenzymes Do Not Depend on the Isoform of the Catalytic Subunit

Zhou

Walter

2003

Journal of Biological Chemistry

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The protein phosphatase 2A holoenzyme is composed of one catalytic C subunit, one regulatory/scaffolding A subunit, and one regulatory B subunit. The core enzyme consists of A and C subunits only. The A and C subunits both exist as two closely related isoforms, ␣ and ␤. The B subunits belong to four weakly related or unrelated families, designated B, B , B؆, and Bٟ, with multiple members in each family. The existence of two A and two C subunit isoforms permits the formation of four core enzymes, A␣C␣, A␣C␤, A␤C␣, and A␤C␤, and each core enzyme could in theory give rise to multiple holoenzymes. Differences between C␣ and C␤ in expression and subcellular localization during early embryonic development have been reported, which imply that C␣ and C␤ have different functions. To address the question of whether these differences might be caused by enzymatic differences between C␣ and C␤, we purified six holoenzymes composed of A␣C␣ or A␣C␤ core enzyme and B subunits from the B, B , or B؆ families. In addition, we purified four holoenzymes composed of A␤C␣ or A␤C␤ and B ␣1 or B؆/PR72. The phosphatase activity of each purified form was assayed using myelin basic protein and histone H1 as substrates. We found that C␣ and C␤ have identical phosphatase activities when associated with the same A and B subunits. Furthermore, no difference was found between C␣ and C␤ in binding A or B subunits. These data suggest that the distinct functions of C␣ and C␤ are not based on differences in enzymatic activity or subunit interaction. The implications for the relationship between the structure and function of C␣ and C␤ are discussed.

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“…And the phosphorylation of this site can be effectively balanced by a phosphatase that is associated with the class C L-type Ca 2+ channel (Ca(v)1.2) (Davare et al 2000). Class C channels (Ca v 1.2) consist of α 1C , α 2 -δ and β 2A .…”

Section: Neurochannelmentioning

confidence: 99%

A review of neurotoxicity of microcystins

Chen

Fan

et al. 2016

Environ Sci Pollut Res

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Cyanobacterial blooms-produced microcystins are secondary metabolites which can accumulate in the food chain and contaminate water, thus posing a potential threat to the health of aquatic animals and even humans. Microcystin toxicity affects not only the liver but also the other organs, i.e., the brain. The serious neurotoxicity effects caused by microcystins then lead to various symptoms. This review focuses on the neurotoxicity of microcystins. Microcystins can cross bloodbrain barrier with the transport of Oatps/OATPs, causing neurostructural, functional, and behavioral changes. In this review, potential uptake mechanisms and neurotoxicity mechanisms are summarized, including neurotransmissions, neurochannels, signal transduction, oxidative stress, and cytoskeleton disruption. However, further researches are needed for detailed studies on signaling pathways and the downstream pathways of neurotoxicity of microcystins.

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Protein Phosphatase 2A Is Associated with Class C L-type Calcium Channels (Cav1.2) and Antagonizes Channel Phosphorylation by cAMP-dependent Protein Kinase

Cited by 165 publications

References 68 publications

p38 Mitogen-Activated Protein Kinase Contributes to Adenosine A₁Receptor-Mediated Synaptic Depression in Area CA1 of the Rat Hippocampus

p38 Mitogen-Activated Protein Kinase Contributes to Adenosine A₁Receptor-Mediated Synaptic Depression in Area CA1 of the Rat Hippocampus

The Formation and Activity of PP2A Holoenzymes Do Not Depend on the Isoform of the Catalytic Subunit

A review of neurotoxicity of microcystins

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Protein Phosphatase 2A Is Associated with Class C L-type Calcium Channels (Cav1.2) and Antagonizes Channel Phosphorylation by cAMP-dependent Protein Kinase

Cited by 165 publications

References 68 publications

p38 Mitogen-Activated Protein Kinase Contributes to Adenosine A1Receptor-Mediated Synaptic Depression in Area CA1 of the Rat Hippocampus

p38 Mitogen-Activated Protein Kinase Contributes to Adenosine A1Receptor-Mediated Synaptic Depression in Area CA1 of the Rat Hippocampus

The Formation and Activity of PP2A Holoenzymes Do Not Depend on the Isoform of the Catalytic Subunit

A review of neurotoxicity of microcystins

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Product

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About

p38 Mitogen-Activated Protein Kinase Contributes to Adenosine A₁Receptor-Mediated Synaptic Depression in Area CA1 of the Rat Hippocampus

p38 Mitogen-Activated Protein Kinase Contributes to Adenosine A₁Receptor-Mediated Synaptic Depression in Area CA1 of the Rat Hippocampus