Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Phosphoproteomic profiling of STK39-mediated phosphorylation on GSK3B

ABSTRACT: This study investigates STK39 (Serine/Threonine Kinase 39)-dependent phosphorylation of GSK3B (Glycogen Synthase Kinase 3 Beta) using affinity purification coupled with mass spectrometry.

ORGANISM(S): Homo Sapiens

SUBMITTER: Zeyang Ding

PROVIDER: PXD062063 | iProX | Thu Mar 20 00:00:00 GMT 2025

REPOSITORIES: iProX

ACCESS DATA

Json Xml

Similar Datasets

GSK3 phosphorylation sites in Lpd

Project description:Neural crest cells are multipotent cells that delaminate from the neuroepithelium, migrating throughout the embryo. Aberrant migration causes developmental defects. Animal models are improving our understanding of neural crest anomalies, but in vivo migration behaviours are poorly understood. Here, we demonstrate that murine neural crest cells display actin-based lamellipodia and filopodia in vivo. Using neural crest-specific knockouts or inhibitors, we show that the serine-threonine kinase Glycogen Synthase Kinase-3 (GSK3), and the cytoskeletal regulator Lamellipodin (Lpd), are required for lamellipodia formation whilst preventing focal adhesion maturation. Lpd is a novel substrate of GSK3 and phosphorylation of Lpd favours interactions with the Scar/WAVE complex (lamellipodia formation) at the expense of VASP and Mena interactions (adhesion maturation and filopodia formation). This improved understanding of cytoskeletal regulation in mammalian neural crest migration has general implications for neural crest anomalies and cancer.

2023-10-05 | PXD044150 | Pride

Cyclic-Di-Nucleotides Trigger ULK1 (ATG1) Phosphorylation of STING to Prevent Sustained Innate Immune Signaling

Project description:Activation of the STING (Stimulator of Interferon Genes) pathway by microbial or self-DNA, as well as cyclic di nucleotides (CDN), results in the induction of numerous genes that suppress pathogen replication and facilitate adaptive immunity. However, sustained gene transcription is rigidly prevented to avoid lethal STING-dependent pro-inflammatory disease by mechanisms that remain unknown. We demonstrate here that after autophagy-dependent STING delivery of TBK1 (TANK-binding kinase 1) to endosomal/lysosomal compartments and activation of transcription factors IRF3 (interferon regulatory factors 3) and NF-κB (nuclear factor kappa beta), that STING is subsequently phosphorylated by serine/threonine UNC-51-like kinase (ULK1/ATG1) and IRF3 function is suppressed. ULK1 activation occurred following disassociation from its repressor adenine monophosphate activated protein kinase (AMPK), and was elicited by CDN’S generated by the cGAMP synthase, cGAS. Thus, while CDN’s may initially facilitate STING function, they subsequently trigger negative-feedback control of STING activity, thus preventing the persistent transcription of innate immune genes. Total RNA obtained from primary STING deficient mouse embryonic fibroblast reconstituted with mSTING (W), S365A variant (A), or S365D variant (D). These cells were transfected with dsDNA (ISD) for 3 hours.

2013-10-10 | E-GEOD-51199 | biostudies-arrayexpress

A Study Evaluating the Combination of Encorafenib and Cetuximab Versus Irinotecan/Cetuximab or Infusional 5-fluorouracil (5-FU)/Folinic Acid (FA)/Irinotecan (FOLFIRI)/Cetuximab in Chinese Patients With BRAF V600E Mutant Metastatic Colorectal Cancer.

Project description:Encorafenib is currently being developed (with or without binimetinib), in combination with cetuximab, for the treatment of adult patients with B-RAF proto-oncogene, serine/threonine kinase V600E mutant (BRAF V600E) metastatic colorectal cancer (mCRC), who have received prior systemic therapy.

| 2386568 | ecrin-mdr-crc

Cyclic-Di-Nucleotides Trigger ULK1 (ATG1) Phosphorylation of STING to Prevent Sustained Innate Immune Signaling

2013-10-10 | GSE51199 | GEO

The kinase GSK-3 alters the repertoire of RNA binding proteins present on lipid metabolism transcripts leading to altered expression in the C. elegans nervous system

Project description:Tissue-specific regulation of gene expression is essential for multicellular organisms, and RNA binding proteins play central roles in these molecular processes. To determine how the Caenorhabditis elegans RNA binding protein ADR-1 regulates tissue-specific gene expression, we profiled the binding targets of ADR-1 in neural cells and assessed the effects of ADR-1 RNA binding on neural gene expression. We identified a cohort of neural transcripts that facilitate lipid synthesis and are directly regulated by ADR-1 RNA binding. To identify cellular factors that influence ADR-1 binding, a forward genetic screen was performed, revealing that the serine/threonine protein kinase, glycogen synthase kinase-3 (GSK-3), inhibits ADR-1 binding to the cohort. Further investigation revealed that RNA binding protein VIG-1, promotes ADR-1 binding to the cohort in a GSK-3-dependent manner. Together, we reveal that interplay between kinases and RNA binding proteins regulates expression of lipid metabolism genes within neural cells, potentially impacting stress resistance and longevity.

2025-03-07 | GSE286247 | GEO

The kinase GSK-3 alters the repertoire of RNA binding proteins present on lipid metabolism transcripts leading to altered expression in the C. elegans nervous system

2025-03-07 | GSE286246 | GEO

Transcription profiling of mouse NIH3T3 cells over-expressing RNA-dependent serine/threonine protein kinase (PKR)PKR

Project description:Global analysis of gene expression in NIH3T3 cells over-expressing RNA-dependent serine/threonine protein kinase (PKR).

2008-06-15 | E-GEOD-682 | biostudies-arrayexpress

Regulation of Glycogen Synthase kinase 3beta by phosphorylation and O-beta-linked N-acetylglucosaminylation: implications on tau protein phosphorylation

Project description:Glycogen synthase kinase 3 (GSK3) plays a pivotal role in signaling pathways related to insulin metabolism and in the pathogenesis of Alzheimer s disease (AD) and other neurodegenerative disorders. More particularly, the GSK3beta isoform is involved in AD-associated tau pathology as one of the major kinases involved in the hyperphosphorylation of the microtubule-associated tau protein, one of the neuropathological hallmarks of AD. As a constitutively active serine/threonine proline-directed kinase, GSK3 is inactivated by Akt/PKB-mediated phosphorylation of Ser9 at the N-terminal disordered domain. Furthermore, GSK3 activity requires for most of its substrates a priming (pre-phosphorylation) by another kinase that allows binding of the substrate in a phosphate-specific pocket near to the active site. It has been shown that GSK3 is also post-translationally modified by O-linked beta-N-acetylglucosaminylation (O-GlcNAcylation) with still unknown functional implications. We have found that binding of the phosphorylated, active form of Akt inhibits GSK3beta kinase activity on both primed and unprimed tau substrates, and Akt-mediated Ser9 phosphorylation restores the GSK3beta kinase activity on primed tau only. Therefore, Ser9 phosphorylation only inactivates GSK3 kinase activity on an unprimed substrate. Additionally, we have shown that GSK3beta is O-GlcNAcylated at multiple sites in both its disordered N- and C-terminal domains including Ser9, but O-GlcNAcylation does not alter kinase activity nor the Akt-mediated regulation of GSK3.

2024-02-09 | MSV000094049 | MassIVE

Genome-wide analysis of gene expression in LIF and LIF plus 2I in C57BL/6 mouse embryonic stem cells (B6 mESCs)

Project description:Analysis of genes induced by 2I condition 2i contains glycogen synthase kinase 3 (GSK3) and mitogen-activated protein kinase kinase (MEK) inhibitors: 3uM Chir99021 and 1uM PD0325901

2013-04-26 | GSE46369 | GEO

Genome-wide analysis of gene expression in LIF and LIF plus 2I in C57BL/6 mouse embryonic stem cells (B6 mESCs)

2013-04-26 | E-GEOD-46369 | biostudies-arrayexpress