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ProteomicsC2 skeletal myotube phosphoproteome
Skeletal muscle is known to adapt dynamically to changes in workload by regulatory processes of the phosphatidylinositide 3-kinase (PI3K)/Akt pathway. We performed a global quantitative phosphoproteomics analysis of contracting mouse C2 myotubes treated with insulin growth factor 1 (IGF-1) or LY2940...
ORGANISM(S): Mus musculus (Mouse) 
2020-05-25 | PXD009117 | Pride
C2 myotubes Phosphoproteomics Pi3k/akt 
ProteomicsIGF-1 stimulated C2 skeletal myotube phosphoproteome
Skeletal muscle is known to adapt dynamically to changes in workload by regulatory processes of the phosphatidylinositide 3-kinase (PI3K)/Akt pathway. We performed a global quantitative phosphoproteomics analysis of contracting mouse C2 myotubes treated with insulin growth factor 1 (IGF-1) as contro...
ORGANISM(S): Mus musculus (Mouse) 
2020-05-25 | PXD016721 | Pride
Silac Phospho-proteomics C2 Myotubes 
ProteomicsQuantitative phosphoproteome of contracting C2 myotubes with pharmacological intervention of the PI3K-AKT-mTOR-S6K and RAF-MEK-ERK-RSK cascades
Various protein kinases are regulating the intracellular signaling network of skeletal muscle cells. Despite that many of the involved kinases are known, their downstream targets have remained largely unexplored. To deepen our understanding of the PI3K-AKT-mTOR-S6K and the RAF-MEK-ERK-RSK signaling ...
ORGANISM(S): Mus musculus (Mouse) 
2023-02-22 | PXD018667 | Pride
Phosphoproteomics Mouse Akt Rsk S6k Skeletal muscle Lc-ms/ms 
ProteomicsLabel-free global phosphoproteomics experiment using PI3K-AKT-mTOR-S6K and RAF-MEK-ERK-RSK pathway activation and inhibition
The signaling network of skeletal muscle cells is controlled by a variety of protein kinases. Although many kinases are known players, their downstream targets are still largely unexplored. To gain further knowledge about the PI3K-AKT-mTOR-S6K and the RAF-MEK-ERK-RSK signaling networks in myotubes, ...
ORGANISM(S): Mus musculus (Mouse) 
2023-02-22 | PXD029678 | Pride
Phosphoproteomics Mouse Akt Rsk Ms S6k Skeletal muscle 
UnknownPancreatic β-cells package double C2-like domain beta protein into extracellular vesicles via tandem C2 domains.
Not available
S-EPMC11532064 | biostudies-literature
UnknownSatellite cells delivered in their niche efficiently generate functional myotubes in three-dimensional cell culture.
Not available
S-EPMC6141091 | biostudies-literature
ProteomicsFlnc d18-21/d1-3 pulldown experiments
The actin-binding protein filamin c (FLNc) is a key mediator in the response of skeletal muscle cells to mechanical stress. In addition to its function as a structural scaffold, FLNc acts as a signaling adaptor which is phosphorylated at S2234 in its mechanosensitive domain 20 (d20) through AKT. Her...
ORGANISM(S): Homo sapiens (Human) 
2025-05-07 | PXD053236 | Pride
Ap-ms Flnc d18-21 interactome C2 cells/myotubes 
ProteomicsValidation of known and novel AKT, S6K and RSK targets by targeted MS
Based on the global SILAC and label-free phosphoproteomics experiments, we generated an inclusion list for validation of known and novel AKT, RSK and S6K targets containing the RxRxxp[ST] motif. Samples were analyzed by targeted MS using PRM.
ORGANISM(S): Mus musculus (Mouse) 
2023-02-22 | PXD029633 | Pride
Phosphoproteomics Mouse Akt Rsk Targeted ms S6k Skeletal muscle 
UnknownThe Switch from NF-YAl to NF-YAs Isoform Impairs Myotubes Formation.
Not available
S-EPMC7140862 | biostudies-literature
TranscriptomicsBAIBA in human skeletal myocytes
The metabolite beta-aminoisobutyric acid (BAIBA) as an exercise-induced muscle-derived signal regulating adipose tissue metabolism during exercise. Here, we determine that BAIBA mimics aerobic exercise training effects on human skeletal myocytes.
ORGANISM(S): Homo sapiens 
2026-06-22 | E-MTAB-14746 | biostudies-arrayexpress
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