Expression and Characterization of Rat Protein Phosphatases-1α, -1γ1, -1γ2, and -1δ

Zhang, Z.J.; Bai, Ge; Shima, Masasuke; Zhao, Sumin; Nagao, Minako; Lee, E.Y.C.

doi:10.1006/abbi.1993.1301

Cited by 59 publications

(44 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…OA-resistant PPs, PP2Ba and PP2C, have a tyrosine residue at the codon corresponding to 269 of PP2Aa, and all of the PP1 catalytic subunits, PPla, PPMyl, and PPly2, and PP18, which are less sensitive to OA, have phenylalanine, the most OA-sensitive PPs, PP2Aa, PP2Af8, and PPX, having cysteine ( Fig. 6) (3,4,26). This observation supports the idea that cysteine encoded at codon 269 may be essential for the high sensitivity to OA.…”

Section: Discussionmentioning

confidence: 99%

“…Okadaic acid (OA), a fatty acid polyether, inhibits these PPs to different extents (2). It inhibits the PP2A form most strongly, causing complete inhibition at 1 nM (1), while it inhibits the PP1 enzyme moderately, with an IC50 of about 50 nM (3), PP2B is even less sensitive, and PP2C is not inhibited (1). In addition to these four major PPs, PPX was recently found to be ubiquitously expressed in various tissues and to be as sensitive to OA as PP2A (4).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Characterization of the PP2A alpha gene mutation in okadaic acid-resistant variants of CHO-K1 cells.

Shima

Tohda

Aonuma

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Okadaic acid (OA)-resistant variants of Chinese hamster ovary cells, clones CHO/OAR6-6 and CHO/OAR2-3, were isolated from a CHO-K1 culture. These variant cells were 17-to 26-fold more i t to OA than the parental cells. The phosphorylase phosphatase activity of the variant cell extracts was 2-to 4-fold more resistant to OA than that ofthe parental cells in the presence of inhibitor 2, a specific inhibitor of type 1 protein serine/threonine phosphatase (PP1

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Characterization of the PP2A alpha gene mutation in okadaic acid-resistant variants of CHO-K1 cells.

Shima

Tohda

Aonuma

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…Preparation of PP1␣-Recombinant PP1␣ was expressed in Escherichia coli (26) and purified as described previously (27). The preparation was further purified by gel filtration on a Sephacryl S-200 column (1.5 ϫ 60 cm).…”

Section: Methodsmentioning

confidence: 99%

A Protein Phosphatase-1-binding Motif Identified by the Panning of a Random Peptide Display Library

Zhao

Lee

1997

Journal of Biological Chemistry

133

125

View full text Add to dashboard Cite

An unusually large number of regulatory or targeting proteins that bind to the catalytic subunit of protein phosphatase-1 have been recently reported. This can be explained by their possession of a common protein motif that interacts with a binding site on protein phosphatase-1. The existence of such a motif was established by the panning of a random peptide library in which peptide sequences are displayed on the Escherichia coli bacterial flagellin protein for bacteria that bound to protein phosphatase-1. There were 79 isolates containing 46 unique sequences with the conserved motif VXF or VXW, where X was most frequently His or Arg. In addition, this sequence was commonly preceded by 2-5 basic residues and followed by 1 acidic residue. This study demonstrates that binding to protein phosphatase-1 can be conferred to a protein by the presentation of a peptide motif on a surface loop. This binding motif is found in a number of protein phosphatase-1-binding proteins.Protein phosphatase-1, originally studied in the context of glycogen metabolism as the enzyme that converts phosphorylase a to phosphorylase b (1), has been implicated in the regulation of a number of important cellular processes (for reviews, see Refs. 2 and 3). Biochemical studies have revealed that it consists of a catalytic subunit (4 -7) of 37 kDa (PP1) 1 that forms a number of heterodimeric enzymes with different subunits, which include a glycogen-binding subunit, a myosin-binding subunit (8), and inhibitor-2 (9). These subunits function to target the catalytic subunit to the subcellular or molecular proximity of its substrates and may serve to provide regulation of activity as well as modulation of substrate specificity (8). In addition, PP1 is regulated by several inhibitory proteins; these include inhibitor-1 (10), DARPP-32 (10), inhibitor-2 and NIPP (a nuclear inhibitory protein) (11). The use of the yeast twohybrid system has led to the discovery of a surprisingly large number of PP1-binding proteins. Mammalian PP1-binding proteins include the retinoblastoma gene product (12), HSP78 (13), p53BP2 (14), splicing factor PSF (15), ribosomal protein L5 (16), herpesvirus ␥ 1 34.5 protein (17), and HOX11 (18). In yeast, over a dozen genes that encode PP1-binding proteins have been identified, based largely on the use of a two-hybrid screen. These include genes that are variously required for control of glycogen metabolism, glucose repression, meiosis and/or sporulation, and mitotic cell cycle regulation (19 -21). Thus, PP1 is unusual in that this single enzyme is involved in the regulation of a number of diverse cellular processes.Few, if any, of the PP1 proteins share any major sequence identity, although examination of different glycogen-binding subunits has revealed the presence of two small regions of sequence similarity that is shared between several glycogenbinding proteins (20,(22)(23)(24)(25). The unusually large number of PP1-binding proteins that have been described suggests either that PP1 contains a motif that is recognized by a common...

show abstract

“…In the ATP/Mg-dependent enzyme, which is a 1:1 complex of PP1 with inhibitor 2, PP1 is present as an inactive or latent enzyme that is reversibly stimulated by Mn 2ϩ (Villa-Moruzzi et al, 1984). All recombinant forms of PP1 expressed in Escherichia coli, including the four known isoforms, are dependent on Mn 2ϩ for activity (Zhang et al, 1992(Zhang et al, , 1993aAlessi et al, 1993). Zhang et al (1993b) have suggested that the recombinant enzyme represents the conformer that is present in the PP1-inhibitor 2 complex.…”

mentioning

confidence: 99%

Activation of Protein Phosphatase 1

Chu

Lee

Schlender

1996

Journal of Biological Chemistry

View full text Add to dashboard Cite

Expression and Characterization of Rat Protein Phosphatases-1α, -1γ1, -1γ2, and -1δ

Cited by 59 publications

References 0 publications

Characterization of the PP2A alpha gene mutation in okadaic acid-resistant variants of CHO-K1 cells.

Characterization of the PP2A alpha gene mutation in okadaic acid-resistant variants of CHO-K1 cells.

A Protein Phosphatase-1-binding Motif Identified by the Panning of a Random Peptide Display Library

Activation of Protein Phosphatase 1

Contact Info

Product

Resources

About