Cátia Igreja

Regulation and post-translational modification of gene expression in nematodes

Max Planck Insitute for Biology
Faculty in: TIPP

Vita

  • Diploma at the University of Lisbon, 1997-2002
  • PhD studies at the University of Lisbon, 2003-2007
  • Postdoctoral fellow at the MPI for Biology, 2007-2014
  • Project Leader, Department of Biochemistry, MPI for Biology, 2014-2020
  • Project Leader, Department for Integrative Evolutionary Biology, MPI for Biology, since 2020

Research Interest

Environmental changes shape developmental and behavioral traits in the nematode Pristionchus pacificus. The molecular mechanisms associated with such phenotypic plasticity are under scrutiny at the Sommerlab. I have spent the last years studying how eukaryotic cells control messenger RNA (mRNA) and protein levels. As a new member and group leader of the Department for Integrative Evolutionary Biology, I intent to apply my knowledge on RNA metabolism and proteins to investigate the regulation of gene expression and plastic traits in P. pacificus. Our approach is interdisciplinary, combining biochemistry, molecular and cellular biology with in vivo manipulation and characterization.

The mouth-form gene network developmentally controls the acquisition of alternative feeding structures in P. pacificus according to environmental cues. This network is enriched in genes encoding proteins with distinct enzymatic activity. To date, our knowledge on the expression, activity and substrates of these enzymes is still limited. To understand their role in the acquisition of a specific mouth-form, we intent to characterize the expression and functions of different enzymes in P. pacificus. We will apply several biochemical, genetic, molecular and proteomic approaches to answer the following questions:

  1. What is the subcellular localization of the enzymes with key roles in mouth-form dimorphism?
  2. How are these enzymes regulated at a post-transcriptional and post-translational level?
  3. What are the substrates modified by these enzymes? Can we measure enzyme activity in vitro and in vivo?

In this project we will explore the time and spatial regulation of the enzymes associated with mouth-form dimorphism, uncover regulatory mechanisms controlling enzyme activity and expression in cells, and identify potential substrates.

 

Available PhD Projects

  • The role of sulfatases in Pristionchus pacificus 
    The Department has an active research program studying the predatory model nematode Pristionchus pacificus with state-of-the-art facilities in molecular biology, biochemistry, nematode genetics, CRISPR-engineering, genomics, and bioinformatics. Our highly interdisciplinary research team works at the interphase between development, evolution and ecology. We investigate among others, the development and evolution of mouth-form plasticity with two alternative, predatory or bacterial feeding morphs. Our results indicate that sulfation, i.e. the biotransformation of molecules between sulphated and unconjugated forms, plays a crucial role in mouth-form plasticity. Although sulfatases perform essential functions from bacteria to humans, their biological roles remain poorly characterized in organisms other than humans. We are currently investigating the importance of sulfatases in phenotypic plasticity and organismal development. We aim at characterizing the expression, regulation, activity and substrates of different sulfatases in the worm using multiple biochemical, molecular, genetic and proteomic approaches. A model system approach can provide unprecedented insight into sulfation and the action and function of sulfatase enzymes.

    We are now looking for an enthusiastic PhD student (m/f/d) to join the department and study the importance of sulfatases in P. pacificus.
    For more information and details of how to apply go to the available projects list.

Selected Reading

  • Igreja, C., and Sommer, R.J. (2022). The Role of Sulfation in Nematode Development and Phenotypic Plasticity. Front Mol Biosci 9, 838148
  • Christie, M., and Igreja, C. (2021). eIF4E-homologous protein (4EHP): a multifarious cap-binding protein. FEBS J
  • Weber, R., Chung, M.Y., Keskeny, C., Zinnall, U., Landthaler, M., Valkov, E., Izaurralde, E., and Igreja, C. (2020). 4EHP and GIGYF1/2 Mediate Translation-Coupled Messenger RNA Decay. Cell Rep 33, 108262.
  • Räsch, F., Weber, R., Izaurralde, E., and Igreja, C. (2020). 4E-T-bound mRNAs are stored in a silenced and deadenylated form. Genes Dev.
  • Grüner, S., Weber, R., Peter, D., Chung, M.Y., Igreja, C., Valkov, E., and Izaurralde, E. (2018). Structural motifs in eIF4G and 4E-BPs modulate their binding to eIF4E to regulate translation initiation in yeast. Nucleic Acids Res 46, 6893-6908.
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