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ProteomicsReprogramming of transcriptome after hormetic heat stress by the endoribonuclease ENDU 2 improves lifespan and stress resistance in C. elegans
Organisms' ability to respond to life-threatening environmental impacts is crucial for their survival. While acute stress responses to unfavorable factors are well known, the physiological consequences of transient stress experiences over time, as well as their underlying mechanisms, are not well un...
ORGANISM(S): Caenorhabditis elegans 
2023-06-29 | PXD041872 | Pride
Ap-ms Heat stress response Hormesis Transcriptional reprogramming Label-free quantification C. elegans Endu-2 
ProteomicsFilamin C domain 18-21 in vitro kinase assay
In vitro kinase assay with human filamin C domain 18-21 recombinantly expressed in E.coli, purified by Ni2+-NTA beads and incubated with PKC alpha, Akt or a combination of both to identify kinase specific phosphorylation sites.
ORGANISM(S): Homo sapiens (Human) Escherichia coli 
2020-05-25 | PXD008893 | Pride
Filamin c Akt In vitro kinase assay Pkb Pkcalpha 
ProteomicsFILIP1 CT pull-down
FILIP1 was identified as potential new filamin C interaction partner by a SILAC-based BioID experiment. Interaction of the two protein via the carboxy-terminal end of FILIP and domain 18-21 of filamin C was prooven by yeast-2-hybrid sreens and dot-blot assays, respectively. To verify this interactio...
ORGANISM(S): Mus musculus (Mouse) 
2022-06-06 | PXD008875 | Pride
C2c12 myotubes Filip1 Filamin c 
ProteomicsFLNc S2233 S2236 PRM analysis
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) 
2020-06-30 | PXD009228 | Pride
Filamin c Akt Pkc Myocytes 
ProteomicsC-terminal FLNc in vivo kinase assay
The Z-disc is a protein-rich structure critically important for myofibril development and integrity. Since a role of the Z-disc for signal integration and transduction was recently suggested, its precise phosphorylation landscape warranted in-depth analysis. We therefore established a site-resolved ...
ORGANISM(S): Mus musculus (Mouse) 
2017-01-02 | PXD004151 | Pride
Flnc pkc gö6976 
ProteomicsBacterial stigmasterol degradation involving radical flavin delta-24 desaturase and molybdenum-dependent C26 hydroxylase
Sterols are ubiquitous membrane constituents that persist to a large extent in the environment due to their water insolubility and chemical inertness. Recently, an oxygenase-independent sterol degradation pathway was discovered in a cholesterol-grown denitrifying bacterium Sterolibacterium (S.) deni...
ORGANISM(S): Sterolibacterium denitrificans 
2024-05-21 | PXD048763 | Pride
Anaerobic metabolism Molybdenum enzyme Steroid degradation Flavin radical enzyme Stigmasterol Desaturasem 
ProteomicsRibosome-inactivation by a widely distributed class of C-tail anchored membrane proteins
Ribosome hibernation is a commonly used strategy that protects ribosomes under unfavorable conditions and regulates developmental processes. Multiple ribosome-hibernation factors have been identified in all domains of life, but due to their structural diversity and the lack of a common mechanism by ...
ORGANISM(S): Escherichia coli Bacteria 
2025-03-04 | PXD052307 | Pride
Translation  stress response Ygam Macrolide antibiotics Yqjd Elab Antimicrobial peptides 
UnknownPhosphoproteomics identifies dual-site phosphorylation in an extended basophilic motif regulating FILIP1-mediated degradation of filamin-C.
Not available
S-EPMC7244511 | biostudies-literature
ProteomicsPhosphoproteomics Identifies Dual-Site Phosphorylation in an Extended Basophilic Motif Regulating FILIP1-mediated Degradation of filamin-C FLNc d18-21 BioID experiment
FLNc, the muscle-specific isoform of the filamin family, is a multi-adaptor protein, comprising 1 amino-terminal actin-binding (ABD) domain followed by 24 immunoglobulin-like (Ig) domains. While FLNc can form homodimers via the last Ig-like domain and thus function as an actin-crosslinker like the o...
ORGANISM(S): Mus musculus (Mouse) 
2021-07-12 | PXD009159 | Pride
Bira Flnc Bioid Myotube 
UnknownMyofibrillar Z-discs Are a Protein Phosphorylation Hot Spot with Protein Kinase C (PKCα) Modulating Protein Dynamics.
Not available
S-EPMC5340999 | biostudies-literature
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