Molecular Cloning and Expression of Mouse Mg2+-Dependent Protein Phosphatase β-4 (Type 2Cβ-4)

Kato, Shunsuke; Terasawa, Takashi; Kobayashi, Toshihide; Ohnishi, Motoko; Sasahara, Yoji; Kusuda, Kazuyuki; Yanagawa, Yuchio; Hiraga, Akira; Matsui, Yasuhisa; Tamura, Shinji

doi:10.1006/abbi.1995.1244

Cited by 28 publications

(38 citation statements)

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“…The NcoI-ScaI fragment was cut out from the expression plasmid pKMC-TK-3, -4 and -5, which harbored PP2C~-3, -4 and -5 [7]. The Ncol site of each of these fragments was given a blunt end by a Klenow fragment and ligated into pGEX-2T which had previously been digested by SmaI; the resultant plasmid was named pGEX-PP2C~-3, -4 and -5.…”

Section: Construction Of Plasmids For Expression Of Gst-pp2c~3 Fusionmentioning

confidence: 99%

“…In a previous study using reverse transcriptase polymerase chain reaction (RT-PCR), we demonstrated that PP2C[3-3, -4 and -5 are expressed specifically in adult mouse testis and intestine and that the expression levels of these three PP2C[3 isoforms in newborn mouse testis are much lower than in adult mouse testis [7]. In this study we investigated the relationship between the expression of PP2C~ isoforms and testicular maturation.…”

Section: Introductionmentioning

confidence: 96%

“…In addition, the isolation of cDNA clones encoding five distinct isoforms of mouse PP2C[3 (PP2C[3-1, -2, -3, -4 and -5) has been also reported [4][5][6][7]. It is likely that these isoforms are the products of alternative splicing of a single pre-mRNA, since they have a common 5' terminal region and differ only in their 3' terminal regions which encode 11-24 amino acids.…”

Section: Introductionmentioning

confidence: 99%

“…It is likely that these isoforms are the products of alternative splicing of a single pre-mRNA, since they have a common 5' terminal region and differ only in their 3' terminal regions which encode 11-24 amino acids. They also differ in the tissue specificity of their expression [5][6][7]. Genes encoding PP2C homologs have also been isolated from other eukaryotic cells [8 14].…”

Section: Introductionmentioning

confidence: 99%

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Differentiation‐dependent enhanced expression of protein phosphatase 2Cβ in germ cells of mouse seminiferous tubules

et al. 1996

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Section: Construction Of Plasmids For Expression Of Gst-pp2c~3 Fusionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Differentiation‐dependent enhanced expression of protein phosphatase 2Cβ in germ cells of mouse seminiferous tubules

et al. 1996

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“…To date, at least six distinct PP2C gene products (2C␣, 2C␤, 2C␥, 2C␦, Wip1, and Ca 2ϩ /calmodulin-dependent protein kinase phosphatase) have been found in mammalian cells (6 -12). In addition, two distinct isoforms of the human PP2C␣ (␣-1 and -2) and five isoforms of the mouse PP2C␤ (␤-1, -2, -3, -4, and -5) have been identified (13)(14)(15)(16). These isoforms are generated in each species as splicing variants of a single pre-mRNA.…”

mentioning

confidence: 99%

Regulation of the TAK1 Signaling Pathway by Protein Phosphatase 2C

Hanada

Ninomiya‐Tsuji

Komaki

et al. 2001

Journal of Biological Chemistry

135

122

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Protein phosphatase type-2C isozymes present in vertebrate retinae: Purification, characterization, and localization in photoreceptors

Klumpp¹,

Selke²,

Fischer³

et al. 1998

J. Neurosci. Res.

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Posttranslational modification of proteins by kinases and phosphatases plays an important role in the regulation of cellular signaling in general and neurochemistry in particular. This also applies to vertebrate photoreceptors where phosphorylation of rhodopsin causes uncoupling from the signal transduction cascade. Functional activity of rhodopsin is restored after substitution of the bleached photopigment 11-cisretinal and by dephosphorylation of the opsin moiety. Phosphatases type-1 and type-2A have been identified in vertebrate retinae. Recently, we have shown by molecular cloning that two isozymes of protein phosphatase type-2C (PP2C, PPM) do exist in retinal tissue. In this report, we have purified PP2Calpha and PP2Cbeta from bovine retinae. Thirty to 40% of PP2C was recovered in the cytosolic fraction. Biochemical properties of native and heterologously expressed recombinant enzymes were similar. Enzymatic activity is strictly dependent on the presence of Mg2+. Addition of Ca2+ ions inhibits Mg2+-sustained activity. Antiserum raised against a C-terminal peptide of PP2Cbeta specifically labeled the outer segments of rod photoreceptor cells. PP2C protein levels were significantly reduced in RCS rats, which develop age-dependent photoreceptor degeneration comparable to the hereditary disease retinitis pigmentosa. Although the retinal substrate(s) remain to be identified, the results suggest that PP2C modulates cellular components of the phototransduction machinery.

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Molecular Cloning and Expression of Mouse Mg2+-Dependent Protein Phosphatase β-4 (Type 2Cβ-4)

Cited by 28 publications

References 0 publications

Differentiation‐dependent enhanced expression of protein phosphatase 2Cβ in germ cells of mouse seminiferous tubules

Differentiation‐dependent enhanced expression of protein phosphatase 2Cβ in germ cells of mouse seminiferous tubules

Regulation of the TAK1 Signaling Pathway by Protein Phosphatase 2C

Protein phosphatase type-2C isozymes present in vertebrate retinae: Purification, characterization, and localization in photoreceptors

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