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ProteomicsSystematic Identification of SHP2 Phosphatase Substrates
Phosphatases play essential roles in normal cell physiology and diseases like cancer. The challenges of studying phosphatases have limited our understanding of their substrates, molecular mechanisms, and unique functions within highly complicate networks. Here we introduce a novel strategy using sub...
ORGANISM(S): Homo sapiens (Human) 
2022-09-20 | PXD028404 | Pride
Phosphoproteomics Tyrosine phosphatase substrates Lc-ms Shp2 
ProteomicsIdentification of PP1c-PPP1R12A Substrates Using K-BIPS (Kinase-Catalyzed Biotinylation to Identify Phosphatase Substrates)
Protein phosphatase 1 regulatory subunit 12A (PPP1R12A) interacts with the catalytic subunit of protein phosphatase 1 (PP1c) to form one of the many protein phosphatase 1 complexes, PP1c-PPP1R12A (or myosin phosphatase). In addition to a well-documented role in muscle contraction, the PP1c-PPP1R12A ...
ORGANISM(S): Rattus norvegicus (Rat) 
2023-10-24 | PXD035213 | Pride
Protein phosphatase 1  pp1  ppp1r12a  chemoproteomics  substrate identification 
ProteomicsIdentification of PP1c-PPP1R12A Substrates Using K-BIPS (Kinase-Catalyzed Biotinylation to Identify Phosphatase Substrates)
Protein phosphatase 1 regulatory subunit 12A (PPP1R12A) interacts with the catalytic subunit of protein phosphatase 1 (PP1c) to form one of the many protein phosphatase 1 complexes, PP1c-PPP1R12A (or myosin phosphatase). In addition to a well-documented role in muscle contraction, the PP1c-PPP1R12A ...
ORGANISM(S): Rattus norvegicus (Rat) 
2023-10-24 | PXD035211 | Pride
Protein phosphatase 1  pp1  ppp1r12a  chemoproteomics  substrate identification 
ProteomicsIdentification of PP1c-PPP1R12A Substrates Using K-BIPS (Kinase-Catalyzed Biotinylation to Identify Phosphatase Substrates)
Protein phosphatase 1 regulatory subunit 12A (PPP1R12A) interacts with the catalytic subunit of protein phosphatase 1 (PP1c) to form one of the many protein phosphatase 1 complexes, PP1c-PPP1R12A (or myosin phosphatase). In addition to a well-documented role in muscle contraction, the PP1c-PPP1R12A ...
ORGANISM(S): Rattus norvegicus (Rat) 
2023-10-24 | PXD035212 | Pride
Protein phosphatase 1  pp1  ppp1r12a  chemoproteomics  substrate identification 
MetabolomicsSCP4-STK35/PDIK1L complex is a dual phospho-catalytic signaling dependency in acute myeloid leukemia
Acute myeloid leukemia (AML) cells rely on phospho-signaling pathways to gain unlimited proliferation potential. Here, we used domain-focused CRISPR screening to identify the nuclear phosphatase SCP4 as a dependency in AML, yet this enzyme is dispensable in normal hematopoietic progenitor cells. Usi...
2025-05-29 | MTBLS3707 | MetaboLights
ProteomicsPhosphatase specificity influences the phosphorylation timing of CDK substrates during the cell cycle
Cell cycle events are ordered by cyclin-dependent kinases (CDKs), which phosphorylate hundreds of substrates. Multiple phosphatases oppose these CDK substrates, yet their collective role in regulating phosphorylation timing in vivo remains unclear. Here, we show that four phosphatases (PP2A-B55, PP2...
ORGANISM(S): Schizosaccharomyces pombe 927 
2025-10-05 | PXD060298 | Pride
Fission yeast Cdk Cell cycle Phosphatase 
ProteomicsVascular endothelial protein tyrosine phosphatase: Identification of novel cell junction-related substrates and a ternary receptor complex with EPHB4 and TIE2
Vascular endothelial protein tyrosine phosphatase (VE-PTP, PTPRB) is a receptor type phosphatase that is crucial for the regulation of endothelial junctions and blood vessel development. VE-PTP regulates vascular integrity by dephosphorylating substrates which are key players in endothelial junction...
ORGANISM(S): Mus musculus (Mouse) 
2019-08-20 | PXD011940 | Pride
Lc-msms Mouse Tyrosine phosphatase Endothelial cells Substrate trapping 
ProteomicsPhactr1/PP1 phosphatase substrates in mouse NIH3T3 fibroblasts
It was previously shown that expression of an activated Phactr1 mutant (Phactr1XXX) that constitutively forms the Phactr1/PP1 phosphatase holoenzyme, induces F-actin rearrangements in NIH3T3 fibroblasts. Expression of the Phactr1 PP1-binding domain (C-terminal) alone is also sufficient to induce suc...
ORGANISM(S): Mus musculus (Mouse) 
2020-10-28 | PXD019977 | Pride
Phosphatase Mouse Phactr1 Fibroblasts 
UnknownIdentification of PP1c-PPP1R12A Substrates Using Kinase-Catalyzed Biotinylation to Identify Phosphatase Substrates.
Not available
S-EPMC10552495 | biostudies-literature
ProteomicsIdentification of PP1-fusion phosphatase substrates
This experiments was designed to identify substrates of holophosphatase complexes of PP1 and its specificity-determining regulator proteins. We generated fusions of Flag-tagged Protein Phosphatase 1 fusions with Phactr1-4, Neurabin, Spinophilin, PPPR15A, PPP1R15B, and PNUTS, in each case including k...
ORGANISM(S): Homo sapiens (Human) 
2025-05-28 | PXD055166 | Pride
Spinophilin Tmt Phosphatase Phosphoproteomics Phactr1 Pp1 
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