Arminja Nadine Kettenbach

This study identifies a bipartite binding mechanism of FAM122A to PP2A-B55, revealing a conserved phosphorylation site involved in cell cycle regulation.

The paper investigates the role of kinases in temperature compensation of circadian rhythms in Neurospora, finding that Casein Kinase I and II have temperature-dependent regulatory roles on FRQ phosphorylation.

This study identifies IRS2's role in protecting cells from mitotic stress through its interaction with PLK1, distinct from its signaling function.

This study shows endocrine therapy induces oxidative stress in ER+ breast cancer cells, making them more susceptible to ferroptosis, suggesting a new therapeutic strategy.

The paper shows CK2 inhibition shifts spindle morphology from meiotic to mitotic-like in Ciona and Xenopus, suggesting CK2 regulates RanGTP-driven microtubule nucleation during fertilization.

The paper identifies RNA-dependent proteins in cell division using R-DeeP, revealing new interactions and phosphorylation events involving AURKA, KIFC1, and TPX2.

The paper identifies CYB5R4 as an evolutionarily conserved reductase that activates PP4 and PP6 by reducing their catalytic metal ions, essential for cell viability under oxidative stress.

This study identifies mitochondrial oxidative phosphorylation as a metabolic vulnerability in endocrine-tolerant persister ER+ breast cancer cells, suggesting therapeutic targeting of mitochondrial function could prevent recurrence.

The paper identifies conserved mechanisms by which PP2A-B55 substrates bind B55 through α-helices and develops a competitive inhibitor to study its function.

This study shows PLK-1 phosphorylation regulates MEX-1 polarization in C. elegans zygotes, similar to its role in POS-1 segregation.

This paper identifies FAM122A as a SLiM-dependent inhibitor of B55/PP2A that competes with substrates to regulate cell cycle progression and checkpoint control.

The paper develops a method using inducible protein degradation and phosphoproteomics to identify kinase-substrate relationships, showing high selectivity and correlation with chemical inhibition.