Protein phosphatase 1--targeted in many directions.

By P. Cohen. Journal of Cell Science, 2002

973 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/1f4bc857943807834dd8c3eaf578ca1aef92e602

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Citations in the corpus

Endoplasmic reticulum stress signaling in disease. (2006, background): “It is now well appreciated that protein phosphatases, including PP1, are represented within the genome by relatively few genes and achieve their specificity through the formation of complexes with regulatory subunits (28).”
Serine/threonine phosphatases: mechanism through structure. (2009, background): “The cellular and physiological functions of PSPs have been extensively discussed in recent reviews (Ceulemans and Bollen, 2004; Cohen, 2002, 2004; Cohen et al., 2005; Gallego and Virshup, 2005; Hinds and Sanchez, 2008; Janssens et al., 2008; Kamenski et al., 2004; Lu and Wang, 2008; Moorhead et…”
Cross Talk Between O-GlcNAcylation and Phosphorylation: Roles in Signaling, Transcription, and Chronic Disease (2011, background): “OGT’s modification of its many substrates is regulated in a manner analogous to that for RNA polymerase II (68) or phosphatase targeting (69).”
Mechanisms of alternative splicing regulation: insights from molecular and genomics approaches (2009, background): “2c ): first, SRp38 is bound and protected by 14-3-3 proteins , and second, protein phosphatase 1 (PP1), which has been shown to target SRp38, is masked by associated proteins, including nuclear inhibitor of PP1 (NIPP1), which had previously been implicated in splicing contro”
Interactome: gateway into systems biology. (2005, background): “Computational prediction utilizing subcellular localization data avoids potential false-positives but can lead to increased false-negatives when a protein is multifunctional and/or active in multiple subcellular compartments or complexes (48,49,108).”
Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins (2007, background): “Thus OGT's protein specificity seems to be regulated similarly to that of phosphatases, such as PP1”
Growth Arrest and DNA Damage-Inducible Protein GADD34 Targets Protein Phosphatase 1α to the Endoplasmic Reticulum and Promotes Dephosphorylation of the α Subunit of Eukaryotic Translation Initiation Factor 2 (2003, methodology): “The ability of WT GADD34(1-674) but not GADD34(1-600) to bind PP1 in the coimmunoprecipitation and affinity isolation assays suggested that the C terminus of GADD34 between amino acids 600 to 674 was crucial for PP1 binding.”
Molecular physiology and pathophysiology of electroneutral cation-chloride cotransporters. (2005, background): “It is known that to perform its specific action on particular serine or threonine residues, PP1 must bind to a motif that should be adjacent to the residues that will be dephosphorylated, thus preventing indiscriminate effects of PP1 in several phosphoproteins (60).”