Results 11 to 20 of about 28,925 (227)
Flexibility in the PP1:spinophilin holoenzyme [PDF]
FEBS Letters, 2010 Protein phosphatase 1 (PP1) interacts with ∼200 regulatory proteins to form holoenzymes, which target PP1 to specific locations and regulate its specificity. While it is known that many PP1 regulatory proteins are dynamic in the unbound state, much less is known about the residual flexibility after PP1 holoenzyme formation.
Ragusa, Michael J. +4 more
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Structural Signature of the MYPT1−PP1 Interaction [PDF]
Journal of the American Chemical Society, 2010 Muscle relaxation is triggered by the dephosphorylation of Ser19 in the myosin regulatory light chain. This reaction is catalyzed by the holoenzyme myosin phosphatase (MP), which includes the catalytic subunit protein phosphatase 1 (PP1) and the regulatory targeting subunit (MYPT).
Pinheiro, Anderson S +3 more
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Membrane targeting with palmitoylated lysine added to PP1‐disrupting peptide induces PP1‐independent signaling [PDF]
Journal of Peptide Science, 2023 Protein phosphatase‐1 (PP1) is a ubiquitous enzyme involved in multiple processes inside cells. PP1‐disrupting peptides (PDPs) are chemical tools that selectively bind to PP1 and release its activity. To restrict the activity of PDPs to a cellular compartment, we developed PDP‐Mem, a cell membrane‐targeting PDP.
Jeremy E. Chojnacki +3 more
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Spindle Checkpoint Silencing: PP1 Tips the Balance [PDF]
Current Biology, 2011 The spindle checkpoint is a mitotic surveillance mechanism that delays anaphase until all sister chromatids are correctly attached to microtubules from opposite poles. Recent studies reveal that protein kinase Aurora B is a key regulator of spindle checkpoint activation whereas protein phosphatase PP1 antagonizes Aurora B and induces checkpoint ...
Lesage, Bart +2 more
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PP1 Phosphatase Complexes: Undruggable No Longer [PDF]
Cell, 2018 The identification of inhibitors targeting regulatory subunits of serine/threonine PP1 phosphatases reported by Krzyzosiak et al. is a significant step in expanding the pharmacological regulation of phosphorylation beyond kinases. The selective inhibitor of the R15B phosphatase regulatory subunit, termed Raphin1, protects cells from stress and delays ...
Vagnarelli, P, Alessi, D
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Structural and Functional Analysis of the GADD34:PP1 eIF2α Phosphatase [PDF]
Cell Reports, 2015 The attenuation of protein synthesis via the phosphorylation of eIF2α is a major stress response of all eukaryotic cells. The growth-arrest- and DNA-damage-induced transcript 34 (GADD34) bound to the serine/threonine protein phosphatase 1 (PP1) is the ...
Meng S. Choy +7 more
doaj +4 more sources
PP1:Tautomycetin Complex Reveals a Path toward the Development of PP1-Specific Inhibitors [PDF]
Journal of the American Chemical Society, 2017 Selective inhibitors for each serine/threonine phosphatase (PPP) are essential to investigate the biological actions of PPPs and to guide drug development. Biologically diverse organisms (e.g., cyanobacteria, dinoflagellates, beetles) produce structurally distinct toxins that are catalytic inhibitors of PPPs.
Meng S. Choy +8 more
openaire +2 more sources
Molecular basis for substrate specificity of the Phactr1/PP1 phosphatase holoenzyme
eLife, 2020 PPP-family phosphatases such as PP1 have little intrinsic specificity. Cofactors can target PP1 to substrates or subcellular locations, but it remains unclear how they might confer sequence-specificity on PP1.
Roman O Fedoryshchak +10 more
doaj +1 more source
Protein phosphatase-1 inhibitor-2 promotes PP1γ positive regulation of synaptic transmission
Frontiers in Synaptic Neuroscience, 2022 Inhibitor-2 (I-2) is a prototypic inhibitor of protein phosphatase-1 (PP1), a major serine-threonine phosphatase that regulates synaptic plasticity and learning and memory.
Karl Foley +15 more
doaj +1 more source
Mitotic ER exit site dynamics: insights into blockade of secretion from the ER during mitosis
Molecular & Cellular Oncology, 2020 How ER exit sites disassemble during mitosis is not well understood. Transport ANd Golgi Organization 1 (TANGO1, also known as MIA3), a cargo receptor originally identified for collagens, acts as a hub for ER exit site disassembly under the control of ...
Miharu Maeda, Yukie Komatsu, Kota Saito
doaj +1 more source