Daniel Moreno Andrés Email & Phone Number

North Rhine-Westphalia, Germany

Aachen, North Rhine-Westphalia (Germany)

I am group leader, permanent research scientist and lecturer at the Institute of Biochemistry and Molecular Cell Biology at Uniklinik RWTH Aachen (Germany) with a leading position. My group performs basic research investigating molecular mechanisms that govern chromatin decondensation and nuclear reassembly at late stages of cellular mitosis. We are also interested in how genetic changes in hematopoietic malignancies and solid cancers perturb regulators, checkpoints and molecular features of cell cycle and mitotic progression to induce disease initiation, progression, and increased aggressiveness.

Aachen (Germany)

I am interested in unveiling the mechanisms governing later stages of cellular mitosis, mainly late anaphase and telophase, where chromatin decondenses to acquire its interphase state, which is paramount for keeping normal gene expression, regulation and cell physiology. For this, I aim also to apply the latest high-throughput and high-resolution microscopy technologies to a variety of cell lines and conditions. Using siRNA or drug libraries for screening and CRISPR/Cas-mediated genome engineering for protein-specific OK in validation processes. Among my objectives is also to study cell lines or tissues affected with human diseases since later stages of cellular mitosis are generally poorly understood despite their importance in developmental processes where mitosis is a touchstone.

Friedrich Miescher Laboratory Of The Max Planck Society In Tuebingen, Germany.

Our goal was to shed light on the ill-defined processes of chromatin decondensation after cellular mitosis. In other to address the problem I implemented in our laboratory a microscopy framework that allow us to screen for proteins or drugs involved in our target process with fast and quantitative readouts for chromatin decondensation. We are currently studying in detail the new chromatin decondensation factors using biochemical, cell biological and life cell imaging approaches.

Friedrich Miescher Laboratory Of The Max Planck Society In Tuebingen, Germany.

Our goal was to shed light on the ill-defined processes of chromatin decondensation after cellular mitosis. In other to address the problem I implemented in our laboratory a microscopy framework that allow us to screen for proteins or drugs involved in our target process with fast and quantitative readouts for chromatin decondensation. We are currently studying in detail the new chromatin decondensation factors using biochemical, cell biological and life cell imaging approaches.

Department Of Molecular Genetics And Cell Biology At University Of Ulm, Germany.

Under the project “Quantitative 3D und 4D Zellanalyse in lebenden Organismen" we aimed to developed a method to map protein-protein interactions in time and space in living cells. For that, we developed a methodology based on the Split-Ubiquitin sensor but using the ratio of two auto-fluorescent reporter proteins as signal for interaction. I used the mating of two separated haploid yeast cells, simulating two reaction channels, that initiate the reaction just when the cytoplasm of separated cells get in contact. This allowed me to analyse and track interactions online by two-channel time-lapse microscopy of the diploid cells during their first cell cycle.

Valencia, Spain

Grant: CSIC I3P2005 fellowshipProject: AMP-dependent protein kinase and ubiquitin- proteasome sistemSupervisor: Prof. Dr. Pascual Sanz Bigorra.I studied the functional relationship between AMP-activated kinase (AMPK) and the ubiquitin proteasome system. I found additional evidence of this bi-directional relationship at the very beginning my PhD period by mean of a couple of screenings: a vitro screening for AMPK activator drugs and in vivo two-hybrid screening for protein interactors. In this way, I found that A769662, a novel activator of AMPK, is able to reversibly inhibit the function of the 26S proteasome in an AMPK-independent manner. The novelty here was that, contrary to most proteasome inhibitors until then, A769662 did not affect proteolytic activities of 20S core subunits, thereby defining a novel mechanism of inhibition of proteasome activity. Additionally, I could proof a direct relationship from AMPK with the proteasome via its subunit PSMD11 and with the ubiquitin system. In the latter case, I found that the laforin–malin complex (phosphatase/E3-ubuiqhitin ligase complex involved in Lafora disease), promotes the incorporation of K63-linked ubiquitin chains in AMPK β subunits increasing the steady-state levels of at least AMPKβ subunit.

Postdoc, Mitosis And Mitoric Chromatin Decondensation

Postdoc, Protein Interaction

Phd, Metabolic Illnesses; Lafora Disease; Ubiquitin - Proteasome Pathway

Biochemistry, Biochemistry, B. Sc. Degree In Biochemistry, B. Sc. Degree In Biochemistry

Primary School