A5055833907- Protein Tyrosine Phosphatases
- Protein Kinase Regulation and GTPase Signaling
- RNA and protein synthesis mechanisms
- PI3K/AKT/mTOR signaling in cancer
- Ubiquitin and proteasome pathways
- Iron Metabolism and Disorders
- Advanced biosensing and bioanalysis techniques
- Mass Spectrometry Techniques and Applications
- Advanced Proteomics Techniques and Applications
- 14-3-3 protein interactions
- Trace Elements in Health
- Galectins and Cancer Biology
- RNA modifications and cancer
- Enzyme Structure and Function
- Neonatal Respiratory Health Research
- S100 Proteins and Annexins
- RNA Research and Splicing
University of Freiburg
2017-2024
Thermo Fisher Scientific (Germany)
2023
Heidelberg University
2017-2018
German Cancer Research Center
2018
European Molecular Biology Laboratory
2017-2018
The phosphatases PP1 and PP2A are responsible for the majority of dephosphorylation reactions on phosphoserine (pSer) phosphothreonine (pThr), involved in virtually all cellular processes numerous diseases. catalytic subunits exist cells form holoenzymes, which impart substrate specificity. contribution to recognition substrates is unclear. By developing a phosphopeptide library approach phosphoproteomic assay, we demonstrate that specificity holoenzymes towards pThr basic motifs adjacent...
The sequence context surrounding the AUG start codon of an open reading frame - 'Kozak sequence' affects probability with which a scanning ribosome will recognize and translating there. A significant number transcripts in animals such as Drosophila contain weak Kozak sequences. This is predicted to cause constitutively low translation these transcripts. We study here additional possibility that mRNAs have sequences allow for regulation their response stress or altered cellular signaling....
This strategy identifies PP1 substrate candidates and pathways triggered by modulator treatment, offering a potentially broad applicability of this approach to other enzyme modulators.
Protein phosphatase-1 (PP1)-disrupting peptides (PDPs) are selective chemical modulators of PP1 that liberate the active catalytic subunit from regulatory proteins; thus allowing dephosphorylation nearby substrates. We have optimized original cell-active PDP3 for enhanced stability, and obtained insights into requirements stabilizing this 23-mer peptide cellular applications. The PDP-Nal was used to dissect involvement in MAPK signaling cascade. Specifically, we demonstrated that, human...
Protein phosphatase‐1 ( PP 1) drives a large amount of phosphoSer/Thr protein dephosphorylations in eukaryotes to counteract multiple kinases signaling pathways. The phosphatase requires divalent metal cations for catalytic activity and contains iron naturally. Iron has been suggested have an influence on 1 through Fe 2+ 3+ oxidation states. However, much biochemical all structural data obtained with recombinant containing Mn ions. Purifying iron‐containing from Escherichia coli thus far not...
Phosphoprotein phosphatase-1 (PP1) is a key player in the regulation of phospho-serine (pSer) and phospho-threonine (pThr) dephosphorylation involved large fraction cellular signaling pathways. Aberrant activity PP1 has been linked to many diseases, including cancer heart failure. Besides well-established control by regulatory proteins, an inhibitory function for phosphorylation (p) Thr residue C-terminal intrinsically disordered tail demonstrated. The associated phenotype cell-cycle arrest...
Phosphatase of regenerating liver (PRL)-3 (PTP4A3) has gained much attention in cancer research due to its involvement tumor promoting and metastatic processes. It belongs the protein tyrosine phosphatase (PTP) superfamily is thought follow catalytic mechanism shared by this family, which aside from conserved active-site amino acids includes a glutamic acid residue that usually required for integrity active site PTPs. We noted structures PRL-3, PRL-1, PTEN these residues do not clearly align...
The cover feature picture shows that deinhibition of protein phosphatase-1 (PP1) with PP1-disrupting peptide (PDP) triggers direct dephosphorylation the kinase phosphoMEK followed by indirect phosphoERK. This finding was enabled complementary application PDP-Nal, optimized in this work for enhanced stability and potency, together tyrosine phosphatase inhibition. More information can be found communication M. Köhn et al. on page 66 Issue 1, 2019 (DOI: 10.1002/cbic.201800541).