Results 11 to 20 of about 28,832 (233)

Identification of peptides interfering with the LRRK2/PP1 interaction.

PLoS ONE, 2020
Serine/threonine phosphatases are responsible for modulating the activities of the protein kinases implicated in the development of several pathologies.
Chang Zhi Dong, Heriberto Bruzzoni-Giovanelli, Yanhua Yu, Karim Dorgham, Christophe Parizot, Jean Marc Zini, Jean Yves Brossas, Pierre Tuffery, Angelita Rebollo   +8 more
doaj   +6 more sources

Interrogating PP1 Activity in the MAPK Pathway with Optimized PP1‐Disrupting Peptides [PDF]

ChemBioChem, 2018
AbstractProtein phosphatase‐1 (PP1)‐disrupting peptides (PDPs) are selective chemical modulators of PP1 that liberate the active PP1 catalytic subunit from regulatory proteins; thus allowing the dephosphorylation of nearby substrates. We have optimized the original cell‐active PDP3 for enhanced stability, and obtained insights into the chemical ...
Yansong Wang, Bernhard Hoermann, Karolina Pavic, Malgorzata Trebacz, Pablo Rios, Maja Köhn   +5 more
openaire   +4 more sources

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., Allaire, Marc, Nairn, Angus C., Page, Rebecca, Peti, Wolfgang   +4 more
openaire   +3 more sources

Aurora B opposes PP1 function in mitosis by phosphorylating the conserved PP1-binding RVxF motif in PP1 regulatory proteins [PDF]

Science Signaling, 2018
Phosphorylation within conserved motifs in regulatory subunits controls protein phosphatase 1 (PP1) holoenzyme assembly during mitosis.
Isha Nasa, Scott F. Rusin, Arminja N. Kettenbach, Greg B. Moorhead   +3 more
openaire   +3 more sources

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, Marsh, Joseph A; id_orcid 0000-0003-4132-0628, Forman-Kay, Julie D, Peti, Wolfgang   +3 more
openaire   +5 more sources

Membrane targeting with palmitoylated lysine added to PP1‐disrupting peptide induces PP1‐independent signaling

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, Laura Scheinost, Yansong Wang, Maja Köhn   +3 more
openaire   +4 more sources

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, Qian, Junbin, Bollen, Mathieu   +2 more
openaire   +3 more sources

Bulky PP1 analogs exert cellular effects independently from analog-sensitive kinase inhibition [PDF]

Frontiers in Chemistry
To circumvent the general lack of selectivity of protein kinase inhibitors, a chemical genetics approach has been developed to allow the selective targeting of engineered kinases by bulky ATP analogs, most of which derived from the pyrazolo[3,4-d ...
Coralie Gicquel, Sabine Genicot, Arnaud Comte, Pierre Colas   +3 more
doaj   +2 more sources

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
openaire   +6 more sources

KNL1 Binding to PP1 and Microtubules Is Mutually Exclusive [PDF]

Structure, 2018
The kinetochore scaffold 1 (KNL1) protein coordinates the spindle assembly checkpoint (SAC), a signaling pathway that delays chromosome segregation until all sister chromatids are properly attached to spindle microtubules. Recently, microtubules and protein phosphatase 1 (PP1), which both bind the N-terminal domain of KNL1, have emerged as regulators ...
Mathieu Bollen, Wolfgang Peti, Rebecca Page   +2 more
exaly   +3 more sources