Molecular Cloning and Developmental Regulation Expression of Two Isoforms of the Catalytic Subunit of Protein Phosphatase 2A from Xenopus laevis

1995 ◽  
Vol 215 (2) ◽  
pp. 666-673 ◽  
Author(s):  
C. Vanhoof ◽  
F. Ingels ◽  
X. Cayla ◽  
I. Stevens ◽  
W. Merlevede ◽  
...  
Keyword(s):  
Xenopus Laevis ◽  
Molecular Cloning ◽  
Protein Phosphatase ◽  
Developmental Regulation ◽  
Protein Phosphatase 2A ◽  
Catalytic Subunit ◽  
Phosphatase 2A

scholarly journals Developmental Expression of Protein Phosphatase 2A in the Kidney

1999 ◽  
Vol 10 (8) ◽  
pp. 1737-1745
Author(s):  
ALLEN D. EVERETT ◽  
CHUN XUE ◽  
TAMARA STOOPS
Keyword(s):  
Signal Transduction ◽  
Protein Phosphatase ◽  
Kidney Development ◽  
Developmental Regulation ◽  
Protein Phosphatase 2A ◽  
Catalytic Subunit ◽  
Developmental Expression ◽  
Regulatory Subunit ◽  
Northern Analysis ◽  
Phosphatase 2A

Abstract. Although a number of growth and transcription factors are known to regulate renal growth and development, the signal transduction molecules necessary to mediate these developmental signals are relatively unknown. Therefore, the activity and mRNA and protein expression of the signal transduction molecule protein phosphatase 2A (PP2A) were examined during rat kidney development. Northern analysis of total kidney RNA or Western analysis of kidney protein homogenates from embryonic day 15 to 90-d-old adults demonstrated developmental regulation of the catalytic, major 55-kD B regulatory subunit and A structural subunit with the highest levels of expression in late embryonic and newborn kidneys. Similarly, okadaic acid-inhibitable phosphatase enzyme activity was highest in the embryonic and newborn kidney. To map cell-specific expression of PP2A in the developing kidney, in situ hybridization with a catalytic subunit digoxigenin-labeled cRNA was performed on embryonic day 20 and newborn kidneys. PP2A was found predominately in the nephrogenic cortex and particularly in the developing glomeruli and nonbrush border tubules in the embryonic day 20 and newborn kidneys. Similarly, immunocytochemistry with a specific PP2A catalytic subunit polyclonal anti-peptide antibody demonstrated catalytic subunit protein particularly concentrated in the podocytes of glomeruli in the newborn kidney. In the adult kidney, PP2A protein was no longer detectable except in the nuclei of distal tubular cells. Therefore, the developmental regulation of PP2A activity and protein during kidney development and its mapping to the nephrogenic cortex, developing glomeruli, and tubules suggests a role for PP2A in the regulation of nephron growth and differentiation.

Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit of protein phosphatase 2A

Biochemistry ◽  
1987 ◽  
Vol 26 (23) ◽  
pp. 7215-7220 ◽  
Author(s):  
Stuart R. Stone ◽  
Jan Hofsteenge ◽  
Brian A. Hemmings
Keyword(s):  
Molecular Cloning ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Catalytic Subunit ◽  
Phosphatase 2A

scholarly journals The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo.

1994 ◽  
Vol 269 (23) ◽  
pp. 16311-16317 ◽  
Author(s):  
B. Favre ◽  
S. Zolnierowicz ◽  
P. Turowski ◽  
B.A. Hemmings
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Catalytic Subunit ◽  
Phosphatase 2A

Diversity, developmental regulation and distribution of murine PR55/B subunits of protein phosphatase 2A

2002 ◽  
Vol 16 (11) ◽  
pp. 2039-2048 ◽  
Author(s):  
Karsten Schmidt ◽  
Stefan Kins ◽  
Andreas Schild ◽  
Roger M. Nitsch ◽  
Brian A. Hemmings ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Developmental Regulation ◽  
Protein Phosphatase 2A ◽  
Phosphatase 2A ◽  
B Subunits

Structure and transcriptional regulation of protein phosphatase 2A catalytic subunit genes [Erratum to document cited in CA114(3):18572v]

Biochemistry ◽  
1991 ◽  
Vol 30 (21) ◽  
pp. 5328-5328 ◽  
Author(s):  
Yeesim Khew-Goodall ◽  
Regina E. Mayer ◽  
Francisca Maurer ◽  
Stuart R. Stone ◽  
Brian A. Hemmings
Keyword(s):  
Transcriptional Regulation ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Catalytic Subunit ◽  
Phosphatase 2A

Identification of protein phosphatase 2A as an interacting protein of leucine-rich repeat kinase 2

2016 ◽  
Vol 397 (6) ◽  
pp. 541-554 ◽  
Author(s):  
Panagiotis S. Athanasopoulos ◽  
Wright Jacob ◽  
Sebastian Neumann ◽  
Miriam Kutsch ◽  
Dirk Wolters ◽  
...  
Keyword(s):  
Hela Cells ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Catalytic Subunit ◽  
Sodium Selenate ◽  
Leucine Rich Repeat ◽  
Human Neuroblastoma ◽  
Interacting Protein ◽  
Cellular Degeneration ◽  
Phosphatase 2A

Abstract Mutations in the gene coding for the multi-domain protein leucine-rich repeat kinase 2 (LRRK2) are the leading cause of genetically inherited Parkinson’s disease (PD). Two of the common found mutations are the R1441C and G2019S. In this study we identified protein phosphatase 2A (PP2A) as an interacting partner of LRRK2. We were able to demonstrate that the Ras of complex protein (ROC) domain is sufficient to interact with the three subunits of PP2A in human neuroblastoma SH-SY5Y cells and in HeLa cells. The alpha subunit of PP2A is interacting with LRRK2 in the perinuclear region of HeLa cells. Silencing the catalytic subunit of PP2A by shRNA aggravated cellular degeneration induced by the pathogenic R1441C-LRRK2 mutant expressed in neuroblastoma SH-SY5Y cells. A similar enhancement of apoptotic nuclei was observed by downregulation of the catalytic subunit of PP2A in cultured cortical cells derived from neurons overexpressing the pathogenic mutant G2019S-LRRK2. Conversely, pharmacological activation of PP2A by sodium selenate showed a partial neuroprotection from R1441C-LRRK2-induced cellular degeneration. All these data suggest that PP2A is a new interacting partner of LRRK2 and reveal the importance of PP2A as a potential therapeutic target in PD.

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