Identification of a Novel Phosphatidic Acid Binding Domain in Protein Phosphatase-1†

Biochemistry ◽  
2005 ◽  
Vol 44 (40) ◽  
pp. 13235-13245 ◽  
Author(s):  
Jeffrey A. Jones ◽  
Robert Rawles ◽  
Yusuf A. Hannun
Keyword(s):  
Phosphatidic Acid ◽  
Protein Phosphatase ◽  
Binding Domain ◽  
Protein Phosphatase 1

scholarly journals Prevention of docosahexaenoic acid-induced cytotoxicity by phosphatidic acid in Jurkat leukemic cells: the role of protein phosphatase-1

2001 ◽  
Vol 1541 (3) ◽  
pp. 188-200 ◽  
Author(s):  
Rafat A. Siddiqui ◽  
Laura J. Jenski ◽  
Jacqueline D. Wiesehan ◽  
Michelle V. Hunter ◽  
Richard J. Kovacs ◽  
...  
Keyword(s):  
Docosahexaenoic Acid ◽  
Phosphatidic Acid ◽  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
Leukemic Cells

scholarly journals Phosphatidic Acid Is a Potent And Selective Inhibitor of Protein Phosphatase 1 and an Inhibitor of Ceramide-mediated Responses

1999 ◽  
Vol 274 (30) ◽  
pp. 21335-21341 ◽  
Author(s):  
Katsuya Kishikawa ◽  
Charles E. Chalfant ◽  
David K. Perry ◽  
Alicja Bielawska ◽  
Yusuf A. Hannun
Keyword(s):  
Phosphatidic Acid ◽  
Protein Phosphatase ◽  
Selective Inhibitor ◽  
Protein Phosphatase 1

scholarly journals Identification of the separate domains in the hepatic glycogen-targeting subunit of protein phosphatase 1 that interact with phosphorylase a, glycogen and protein phosphatase 1

1998 ◽  
Vol 336 (3) ◽  
pp. 699-704 ◽  
Author(s):  
Christopher G. ARMSTRONG ◽  
Martin J. DOHERTY ◽  
Patricia T. W. COHEN
Keyword(s):  
Protein Phosphatase ◽  
Glycogen Synthesis ◽  
Liver Glycogen ◽  
Binding Domain ◽  
Protein Phosphatase 1 ◽  
Hepatic Glycogen ◽  
Storage Site ◽  
C Terminus ◽  
Lysine Residues ◽  
High Affinity Binding Site

Deletion and mutational analyses of the rat liver glycogen-targeting subunit (GL) of protein phosphatase 1 (PP1) have identified three separate domains that are responsible for binding of PP1, glycogen and phosphorylase a. The glycogen-binding domain spans the centre of GL between residues 144 and 231 and appears to be distinct from the glycogen-binding (storage) site of phosphorylase. The regulatory high-affinity binding site for phosphorylase a lies in the 16 amino acids at the C-terminus of GL. The PP1-binding domain is deduced to comprise the -RVXF- motif [Egloff, Johnson, Moorhead, Cohen and Barford (1997) EMBO J. 16, 1876–1887] located at residues 61–64 of GL and preceding lysine residues at positions 56, 57 and 59. A possible approach for increasing glycogen synthesis in certain disorders is discussed.

scholarly journals Mapping of the RNA-binding and endoribonuclease domains of NIPP1, a nuclear targeting subunit of protein phosphatase 1

1999 ◽  
Vol 342 (1) ◽  
pp. 13-19 ◽  
Author(s):  
Qiming JIN ◽  
Monique BEULLENS ◽  
Izabela JAGIELLO ◽  
Aleyde VAN EYNDE ◽  
Veerle VULSTEKE ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Rna Binding ◽  
Specific Activity ◽  
Binding Domain ◽  
Protein Phosphatase 1 ◽  
Binding Motif ◽  
Nucleic Acid Binding ◽  
Nuclear Targeting ◽  
Rna Binding Domain ◽  
Endoribonuclease Activity

NIPP1 (351 residues) is a major regulatory and RNA-anchoring subunit of protein phosphatase 1 in the nucleus. Using recombinant and synthetic fragments of NIPP1, the RNA-binding domain was mapped to the C-terminal residues 330-351. A synthetic peptide encompassing this sequence equalled intact NIPP1 in RNA-binding affinity and could be used to dissociate NIPP1 from the nuclear particulate fraction. An NIPP1 fragment consisting of residues 225-351 (Ard1/NIPP1γ), that may be encoded by an alternatively spliced transcript in transformed B-lymphocytes, displayed a single-strand Mg2+-dependent endoribonuclease activity. However, full-length NIPP1 and NIPP1143-351 were not able to cleave RNA, indicating that the endoribonuclease activity of NIPP1 is restrained by its central domain. The endoribonuclease activity was also recovered in the RNA-binding domain, NIPP1330-351, but with a 30-fold lower specific activity. Thus, the endoribonuclease catalytic site and the RNA-binding site both reside in the C-terminal 22 residues of NIPP1. The latter domain does not conform to any known nucleic-acid binding motif.

scholarly journals Targeting Protein Phosphatase 1 (PP1) to the Actin Cytoskeleton: the Neurabin I/PP1 Complex Regulates Cell Morphology

2002 ◽  
Vol 22 (13) ◽  
pp. 4690-4701 ◽  
Author(s):  
Carey J. Oliver ◽  
Ryan T. Terry-Lorenzo ◽  
Elizabeth Elliott ◽  
Wendy A. Christensen Bloomer ◽  
Shi Li ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Actin Cytoskeleton ◽  
Protein Phosphatase ◽  
Binding Domain ◽  
Stress Fibers ◽  
Protein Phosphatase 1 ◽  
In Vivo Studies ◽  
Actin Binding ◽  
Binding Motif ◽  
Actin Binding Domain

ABSTRACT Neurabin I, a neuronal actin-binding protein, binds protein phosphatase 1 (PP1) and p70 ribosomal S6 protein kinase (p70S6K), both proteins implicated in cytoskeletal dynamics. We expressed wild-type and mutant neurabins fused to green fluorescent protein in Cos7, HEK293, and hippocampal neurons. Biochemical and cellular studies showed that an N-terminal F-actin-binding domain dictated neurabin I localization at actin cytoskeleton and promoted disassembly of stress fibers. Deletion of the C-terminal coiled-coil and sterile alpha motif domains abolished neurabin I dimerization and induced filopodium extension. Immune complex assays showed that neurabin I recruited an active PP1 via a PP1-docking sequence,457KIKF460. Mutation of the PP1-binding motif or PP1 inhibition by okadaic acid and calyculin A abolished filopodia and restored stress fibers in cells expressing neurabin I. In vitro and in vivo studies suggested that the actin-binding domain attenuated protein kinase A (PKA) phosphorylation of neurabin I. Modification of a major PKA site, serine-461, impaired PP1 binding. Finally, p70S6K was excluded from neurabin I/PP1 complexes and required the displacement of PP1 for recruitment to neurabin I. These studies provided new insights into the assembly and regulation of a neurabin I/PP1 complex that controls actin rearrangement to promote spine development in mammalian neurons.

Regulation of glycogen synthase and protein phosphatase-1 by hexosamines

Diabetes ◽  
1996 ◽  
Vol 45 (3) ◽  
pp. 322-327 ◽  
Author(s):  
E. D. Crook ◽  
D. A. McClain
Keyword(s):  
Protein Phosphatase ◽  
Glycogen Synthase ◽  
Protein Phosphatase 1
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