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M

Maria M. Drerup

Researcher at University of Münster

Publications -  4
Citations -  545

Maria M. Drerup is an academic researcher from University of Münster. The author has contributed to research in topics: Protein kinase A & Expression cassette. The author has an hindex of 4, co-authored 4 publications receiving 390 citations.

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The Calcineurin B-Like Calcium Sensors CBL1 and CBL9 Together with Their Interacting Protein Kinase CIPK26 Regulate the Arabidopsis NADPH Oxidase RBOHF

TL;DR: A direct interconnection between CBL-CIPK-mediated Ca(2+) signaling and ROS signaling in plants is identified and evidence for a synergistic activation of the NADPH oxidase RBOHF is provided by directCa(2+)-binding to its EF-hands and Ca( 2+)-induced phosphorylation by CBL1/9-C IPK26 complexes.
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Fine-tuning of RBOHF activity is achieved by differential phosphorylation and Ca 2+ binding

TL;DR: RBOHF is identified as a convergence point targeted by a complex regulatory network of kinases and phosphatases that allows for fine-tuning of plant reactive oxygen species (ROS) production by RBOHF in response to different stimuli and in diverse physiological processes.
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A New β-Estradiol-Inducible Vector Set that Facilitates Easy Construction and Efficient Expression of Transgenes Reveals CBL3-Dependent Cytoplasm to Tonoplast Translocation of CIPK5

TL;DR: A new set of 57 vectors that enable transgene expression in transiently or stably transformed cells and investigated the influence of CBL (Calcineurin B-like) protein expression on the subcellular localization of CIPKs, finding that induced co-expression of C BL3 is fully sufficient for dynamic translocation of C IPK5 from the cytoplasm to the tonoplast.
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CIPK11-Dependent Phosphorylation Modulates FIT Activity to Promote Arabidopsis Iron Acquisition in Response to Calcium Signaling.

TL;DR: It is proposed that Ca2+-triggered CBL1/9-mediated activation of CIPK11 and subsequent phosphorylation of FIT shifts inactive into active FIT, allowing regulatory protein interactions in the nucleus and represents an environment-sensing mechanism to adjust nutrient uptake.