Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize  the interaction of PP-1 with binding proteins

Kwon, Young Guen; Huang, Hsien Bin; Desdouits, Frédéric; Girault, Jean‐Antoine; Greengard, Paul; Nairn, Angus C.

doi:10.1073/pnas.94.8.3536

Cited by 117 publications

(99 citation statements)

References 43 publications

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“…Thus, our study revealed that PP1 not only stabilizes MT attachment by dephosphorylating Aurora-B substrates at KTs 18,28-30 but also induces plate thinning by dephosphorylating Kif18A. At the same time, this finding establishes Kif18A as the first Cdk1 substrate-apart from PP1 itself [37][38][39] -that is directly dephosphorylated by PP1 demonstrating that PP1 can act as an antagonist of not only Aurora-B but also Cdk1. Dephosphorylation of Kif18A by PP1 depends on a conserved PP1-binding motif located in the Cterminus of Kif18A (Fig.…”

Section: Discussionsupporting

confidence: 58%

Pre-anaphase chromosome oscillations are regulated by the antagonistic activities of Cdk1 and PP1 on Kif18A

et al. 2014

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Section: Discussionsupporting

confidence: 58%

Pre-anaphase chromosome oscillations are regulated by the antagonistic activities of Cdk1 and PP1 on Kif18A

et al. 2014

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“…Many of these proteins share a canonical tetrapeptide motif, RVXF, which represents an important PP1-binding domain (37,38 (11), which may approximate to the RVXF motif. However, no such sequence was found in I 1 PP2A (10), which functioned in essentially the same manner as I 2 PP2A to stimulate the histone H1 and MBP phosphatase activity of PP1 C (Figs.…”

Section: Discussionmentioning

confidence: 99%

Protein Phosphatase 2A Inhibitors, I1PP2A and I2PP2A, Associate with and Modify the Substrate Specificity of Protein Phosphatase 1

Katayose

Al-Murrani

et al. 2000

Journal of Biological Chemistry

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“…With one exception, these all exhibit the VXF motif, and only one occurrence of the VXW sequence was found. Both inhibitor-1 and DARPP-32 contain sequences at their N termini (KIQF) that are similar to the RVXF motif and that are required for inhibition of PP1 (35,36). Interestingly, the results of the random peptide screen did not yield any substitution of Val for Ile.…”

Section: Table I Alignment Of Peptide Sequences That Bind To Pp1mentioning

confidence: 99%

“…It remains a possibility that binding of variants of the PP1-binding motif could produce differential effects on either activity or substrate specificity. In this regard, it is of interest to note that both inhibitor-1 and DARPP-32 contain sequences at their N termini (KIQF) that are similar to the RVXF motif and that are required for inhibition of PP1 (35,36). Irrespective of whether occupancy of the VXF binding site can affect either activity or substrate specificity, there is support for a model in which a high affinity interaction with PP1 involves at least two binding sites of lower affinity, as has been suggested for inhibitor-1 and DARPP-32 (34 -36).…”

Section: Table I Alignment Of Peptide Sequences That Bind To Pp1mentioning

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

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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...

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Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins

Abstract: The

Cited by 117 publications

References 43 publications

Pre-anaphase chromosome oscillations are regulated by the antagonistic activities of Cdk1 and PP1 on Kif18A

Pre-anaphase chromosome oscillations are regulated by the antagonistic activities of Cdk1 and PP1 on Kif18A

Protein Phosphatase 2A Inhibitors, I1PP2A and I2PP2A, Associate with and Modify the Substrate Specificity of Protein Phosphatase 1

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

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