Detection of multiple splice variants of the nuclear protein phosphatase 1 regulator sds22 in rat liver nuclei

2002 ◽  
Vol 80 (6) ◽  
pp. 811-815 ◽  
Author(s):  
Hue T Tran ◽  
Dave Bridges ◽  
Annegret Ulke ◽  
Greg B.G Moorhead
Keyword(s):  
Rat Liver ◽  
Protein Phosphatase ◽  
Nuclear Protein ◽  
Splice Variants ◽  
Nuclear Extract ◽  
Nuclear Proteins ◽  
Protein Phosphatase 1 ◽  
N Terminus ◽  
Liver Nuclei ◽  
Different Levels

Antipeptide antibodies generated against the N terminus of the protein phosphatase 1 (PP1) binding protein sds22 detected at least four forms of the protein in a rat liver nuclear extract. Four of these immunoreactive bands likely correspond to four predicted forms of sds22 that are generated by alternative splicing. These four proteins are expressed at different levels and appear to be localized exclusively in the nucleus, and two of these proteins copurify with PP1 on the protein phosphatase affinity matrix microcystin–Sepharose. Two higher molecular mass nuclear proteins that are immunoreactive with the sds22 antibodies also copurify on microcystin–Sepharose and may be novel forms of sds22 expressed in mammalian cells.Key words: sds22, protein phosphatase 1 (PP1), nucleus, microcystin–Sepharose.

scholarly journals Identification of high levels of protein phosphatase-1 in rat liver nuclei

FEBS Letters ◽  
1986 ◽  
Vol 203 (2) ◽  
pp. 197-202 ◽  
Author(s):  
Jeff Kuret ◽  
Heather Bell ◽  
Philip Cohen
Keyword(s):  
Rat Liver ◽  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
Rat Liver Nuclei ◽  
Liver Nuclei

scholarly journals Identification of sds22 as an inhibitory subunit of protein phosphatase-1 in rat liver nuclei

FEBS Letters ◽  
1997 ◽  
Vol 402 (2-3) ◽  
pp. 141-144 ◽  
Author(s):  
Anca Dinischiotu ◽  
Monique Beullens ◽  
Willy Stalmans ◽  
Mathieu Bollen
Keyword(s):  
Rat Liver ◽  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
Rat Liver Nuclei ◽  
Liver Nuclei

scholarly journals Subunit Structure and Regulation of Protein Phosphatase-1 in Rat Liver Nuclei

1995 ◽  
Vol 270 (29) ◽  
pp. 17257-17263 ◽  
Author(s):  
Izabela Jagiello ◽  
Monique Beullens ◽  
Willy Stalmans ◽  
Mathieu Bollen
Keyword(s):  
Rat Liver ◽  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
Subunit Structure ◽  
Rat Liver Nuclei ◽  
Liver Nuclei

scholarly journals Modulation by Exogenous Histones of Phosphorylation of Non-Histone Nuclear Proteins in Isolated Rat Liver Nuclei

1973 ◽  
Vol 248 (21) ◽  
pp. 7595-7600
Author(s):  
Edward M. Johnson ◽  
Giorgio Vidali ◽  
Virginia C. Littau ◽  
Vincent G. Allfrey
Keyword(s):  
Rat Liver ◽  
Nuclear Proteins ◽  
Isolated Rat Liver ◽  
Rat Liver Nuclei ◽  
Liver Nuclei ◽  
Isolated Rat

Nuclear Protein Phosphatase 1 α (PP1A) Expression is Associated with Poor Prognosis in p53 Expressing Glioblastomas

2015 ◽  
Vol 22 (2) ◽  
pp. 287-292 ◽  
Author(s):  
Arun H. Shastry ◽  
Balaram Thota ◽  
Mallavarapu R. Srividya ◽  
Arimappamagan Arivazhagan ◽  
Vani Santosh
Keyword(s):  
Protein Phosphatase ◽  
Poor Prognosis ◽  
Nuclear Protein ◽  
Protein Phosphatase 1

In vitro transfer of N,N′-diacetylchitobiose to glycoproteins in rat liver nuclei

1992 ◽  
Vol 70 (8) ◽  
pp. 677-683 ◽  
Author(s):  
Jacques Frot—Coutaz ◽  
Agnès Degiuli ◽  
Marie-Bénédicte Martel ◽  
Robert Létoublon
Keyword(s):  
Rat Liver ◽  
Biological Significance ◽  
Nuclear Proteins ◽  
Direct Transfer ◽  
Rat Liver Nuclei ◽  
Liver Nuclei

This work demonstrates that (N-acetyl[14C]glucosamine)2 is transferred from dolichyl pyrophosphate – (N-acetyl[14C]glucosamine)2 to endogenous nuclear glycoproteins. The (N-acetyl[l4C]gIucosamine)2 moiety is N-linked, since it can be released from the tryptic glycopeptides by N-glycosidase F and by hydrazinolysis, but not by β-elimination. The biological significance of this direct transfer of N, N′-diacetylchitobiose to nuclear proteins remains to be elucidated.Key words: nucleus, nuclear glycoproteins, nuclear N-acetylglucosaminyltransferase, N,N′ -diacetylchitobiose.

scholarly journals Nuclear-envelope vesicles as a model system to study nucleocytoplasmic transport. Specific uptake of nuclear proteins

1987 ◽  
Vol 241 (1) ◽  
pp. 213-219 ◽  
Author(s):  
N Riedel ◽  
H Fasold
Keyword(s):  
Nuclear Envelope ◽  
Rat Liver ◽  
Protein Translocation ◽  
High Mobility ◽  
Preceding Paper ◽  
Nucleocytoplasmic Transport ◽  
Nuclear Proteins ◽  
Rat Liver Nuclei ◽  
Liver Nuclei

In the preceding paper [Riedel & Fasold (1987) Biochem. J. 241, 203-212] we have described a procedure for the preparation of nuclear-envelope vesicles (NE vesicles) from rat liver nuclei. These vesicles, which are largely free of components of the nuclear interior, were employed in an assay system in vitro to study protein translocation across the NE. We found that nuclear proteins such as histones, high-mobility-group proteins and acidic chromosomal proteins are specifically taken up and accumulated in the NE vesicles, whereas there is little or no affinity for non-nuclear proteins like immunoglobulin, myoglobin and cytochrome c. The kinetics of histone uptake into the NE vesicles are similar to those obtained for whole rat liver nuclei, and comparative studies with non-vesicular NEs prepared by deoxyribonuclease I-treatment (DNAase-NEs) indicate that the NE of the vesicles affects the uptake kinetics and increases the capacity for nuclear proteins. The uptake of histones into NE vesicles, but not the binding to DNAase-NEs, can be stimulated by GTP and GDP. Furthermore, we found that even very large molecules can be entrapped in the vesicles during their preparation. These results indicate that the NE vesicles might provide a useful system in vitro with which to investigate the structures and mechanisms involved in protein translocation across the NE.

scholarly journals Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores.

1987 ◽  
Vol 104 (2) ◽  
pp. 189-200 ◽  
Author(s):  
D R Finlay ◽  
D D Newmeyer ◽  
T M Price ◽  
D J Forbes
Keyword(s):  
Rat Liver ◽  
Protein Transport ◽  
Nuclear Protein ◽  
Nuclear Transport ◽  
Nuclear Pore ◽  
Major Mechanism ◽  
Rat Liver Nuclei ◽  
Egg Extract ◽  
Liver Nuclei

Selective transport of proteins is a major mechanism by which biochemical differences are maintained between the cytoplasm and nucleus. To begin to investigate the molecular mechanism of nuclear transport, we used an in vitro transport system composed of a Xenopus egg extract, rat liver nuclei, and a fluorescently labeled nuclear protein, nucleoplasmin. With this system, we screened for inhibitors of transport. We found that the lectin, wheat germ agglutinin (WGA), completely inhibits the nuclear transport of fluorescently labeled nucleoplasmin. No other lectin tested affected nuclear transport. The inhibition by WGA was not seen when N-acetylglucosamine was present and was reversible by subsequent addition of sugar. When rat liver nuclei that had been incubated with ferritin-labeled WGA were examined by electron microscopy, multiple molecules of WGA were found bound to the cytoplasmic face of each nuclear pore. Gel electrophoresis and nitrocellulose transfer identified one major and several minor nuclear protein bands as binding 125I-labeled WGA. The most abundant protein of these, a 63-65-kD glycoprotein, is a candidate for the inhibitory site of action of WGA on nuclear protein transport. WGA is the first identified inhibitor of nuclear protein transport and interacts directly with the nuclear pore.

Inhibition of nuclear-protein phosphorylation in vitro by beryllium

1983 ◽  
Vol 3 (10) ◽  
pp. 955-962 ◽  
Author(s):  
Betsan E. Williams ◽  
David N. Skilleter
Keyword(s):  
Protein Phosphorylation ◽  
Rat Liver ◽  
Cyclic Nucleotide ◽  
Binding Sites ◽  
Nuclear Protein ◽  
Adult Rat ◽  
Liver Nuclei ◽  
Protein Dephosphorylation ◽  
Independent Protein

Endogenous cyclic-nucleotide-independent protein phosphorylation by ATP at pH 6.5 in adult rat liver nuclei in vitro is inhibited by beryllium (Be2+), but under the same conditions nuclear-protein dephosphorylation appears to be insensitive to Be2+. Prior incubation of nuclei with Be2+ is necessary to demonstrate the inhibition of phosphorylation, which increases as the pH is decreased from pH 8.0 to 6.5. The extent of inhibition can be related to the level of nuclear Be2+ binding and, evidence suggests, may be caused by direct or indirect interference by Be2+ with Mg2+ binding sites normally required to facilitate protein phosphorylation.

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