ASPP proteins discriminate between PP1 catalytic subunits through their SH3 domain and the PP1 C-tail [PDF]
Serine/threonine phosphatases such as PP1 associate with a large array of subunit proteins, such as ASPP (apoptosis-stimulating protein of p53) to achieve selective targeting.
M. Teresa Bertran +14 more
doaj +9 more sources
Identification of peptides interfering with the LRRK2/PP1 interaction. [PDF]
Serine/threonine phosphatases are responsible for modulating the activities of the protein kinases implicated in the development of several pathologies.
Chang Zhi Dong +8 more
doaj +6 more sources
Interrogating PP1 Activity in the MAPK Pathway with Optimized PP1‐Disrupting Peptides [PDF]
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 +5 more
openaire +5 more sources
Aurora B opposes PP1 function in mitosis by phosphorylating the conserved PP1-binding RVxF motif in PP1 regulatory proteins [PDF]
Phosphorylation within conserved motifs in regulatory subunits controls protein phosphatase 1 (PP1) holoenzyme assembly during mitosis.
Isha Nasa +3 more
openaire +4 more sources
Bulky PP1 analogs exert cellular effects independently from analog-sensitive kinase inhibition [PDF]
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 +3 more
doaj +2 more sources
KNL1 Binding to PP1 and Microtubules Is Mutually Exclusive [PDF]
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 ...
, Wolfgang Peti, Mathieu Bollen
exaly +3 more sources
ASPPs multimerize protein phosphatase 1. [PDF]
Protein Phosphatase 1 (PP1) activity is thought to be spatiotemporally defined by hundreds of different regulatory subunits, but their mechanisms of action are largely unknown.
Derek T Wei +7 more
doaj +2 more sources
The SDS22:PP1:I3 complex: SDS22 binding to PP1 loosens the active site metal to prime metal exchange
SDS22 and Inhibitor-3 (I3) are two ancient regulators of protein phosphatase 1 (PP1) that regulate multiple essential biological processes. Both SDS22 and I3 form stable dimeric complexes with PP1; however, and atypically for PP1 regulators, they also form a triple complex, where both proteins bind to PP1 simultaneously (SPI complex).
Lucy Robinson, , Kelly Tatchell
exaly +3 more sources
Xenopus Cdc7 executes its essential function early in S phase and is counteracted by checkpoint-regulated protein phosphatase 1 [PDF]
The initiation of DNA replication requires two protein kinases: cyclin-dependent kinase (Cdk) and Cdc7. Although S phase Cdk activity has been intensively studied, relatively little is known about how Cdc7 regulates progression through S phase.
Wei Theng Poh +4 more
doaj +1 more source
Small molecules targeted to a non-catalytic "RVxF" binding site of protein phosphatase-1 inhibit HIV-1. [PDF]
HIV-1 Tat protein recruits host cell factors including CDK9/cyclin T1 to HIV-1 TAR RNA and thereby induces HIV-1 transcription. An interaction with host Ser/Thr protein phosphatase-1 (PP1) is critical for this function of Tat. PP1 binds to a Tat sequence,
Tatiana Ammosova +7 more
doaj +1 more source

