Laureano de la Vega

+44 (0)1382 383990
Discovery Fellow



Laureano de la Vega is a biochemist graduate from the University of Cordoba (Spain), he finished his PhD in Biochemistry in 2007 obtaining the highest degree, Summa Cum Laude, for his work investigating the molecular mechanisms regulating HIV latency. Following this, he moved to Giessen (Germany) to join the team of Prof. Lienhard Schmitz as a postdoctoral researcher from 2007 to 2013. During that time his research was focused on post-translational modifications of HIPK2, an important regulator of cell growth, cell death and differentiation. In 2013 he moved to Dundee where he started his own group focused on the regulation of stress response pathways in cancer.

Research interests

Stress Responses

Organisms need to be able to adapt to change in order to survive, and certain cellular programs (stress response pathways) have evolved to respond to a dynamic environment. Example of stress responses pathways include p53, NRF2, and HSF1 pathways. Stress responses are by definition acute, and their transient activation help normal cells to cope with cellular stresses. Interestingly, there is a large body of evidence showing that, in contrast to normal cells, cancer cells are constitutively under cellular stress (i.e. DNA damage/replication stress, proteotoxic stress, mitotic stress, metabolic stress, and oxidative stress) and they depend on the sustained activation of cytoprotective stress response pathways to survive.

The essential nature of the stress response pathways in cancer cells makes them attractive targets, and thus, a better understanding of how these pathways are regulated could help identify new ways to modulate stress responses to impair cancer cell survival. In that sense, our lab is focused in obtaining a detailed understanding of stress response pathways and their aberrations in cancer. For that, we are interested not only on key master regulators of stress responses (e.g. NRF2, HSF1 or P53) but as well in the upstream regulatory pathways that modulate their activity (i.e. upstream kinases).

HIPK/DYRK family

Homeodomain-Interacting Protein Kinases (HIPKs) are a subfamily of the Dual specificity tYrosine Regulated Kinase (DYRK) family of kinases. These kinases function as hubs for a wide variety of stress signals, ranging from DNA damage and hypoxia to reactive oxygen species and metabolic stress. HIPK/DYRKs function as integrators for these stress signals and modulate different downstream pathways in order to allow cells to cope with these situations. Different posttranslational modifications modulate the activity and physiological role of HIPK/DYRKs, and the study of how their activity is regulated in different pathophysiological scenarios is an important line of investigation in cancer research.

Based on the literature and on previous studies from the lab it has become apparent that HIPK/DYRKs can play a dual role in cancer; either inducing apoptosis or promoting cell survival. While the pathways involved in their tumour suppressor role are relatively well studied, the underlying mechanisms mediating their pro-survival function(s) are not well characterised. Specifically, we are interested in i) understanding how this family of kinases is regulated in cancer cells; ii) identifying novel HIPK/DYRK-regulated pro-survival/oncogenic pathways and iii) to identify the basis for such functional duality in cancer, as it will inform us in which type of cancer or under which conditions (i.e. initial stages of cancer versus well stablished cancers) these kinases can support cancer cell survival and tumour growth.


Laureano currently teaches on the MRes Cancer Biology Course as a module lead, and on the BSc (Hons) level 3 Molecular Biology module and as a Journal Club leader.


Crosstalk between NRF2 and HIPK2 shapes cytoprotective responses
5/2017, Oncogene
Research Output: Contribution To Journal > Article

Transcription factors NRF2 and HSF1 have opposing functions in autophagy
8/2017, Scientific Reports
Research Output: Contribution To Journal > Article

Heat Shock Factor 1 is a Substrate for p38 Mitogen-Activated Protein Kinases
6/2016, Molecular and Cellular Biology
Research Output: Contribution To Journal > Article

New insights into the role of histone deacetylases as coactivators of inflammatory gene expression
7/2015, Antioxidants & Redox Signaling
Research Output: Contribution To Journal > Article

Homeodomain-interacting protein kinase 2-dependent repression of myogenic differentiation is relieved by its caspase-mediated cleavage
6/2013, Nucleic Acids Research
Research Output: Contribution To Journal > Article

HIPK2 kinase activity depends on cis-autophosphorylation of its activation loop
4/2012, Journal of Molecular Cell Biology
Research Output: Contribution To Journal > Article

A Redox-Regulated SUMO/Acetylation Switch of HIPK2 Controls the Survival Threshold to Oxidative Stress
5/2012, Molecular Cell
Research Output: Contribution To Journal > Article

Control of nuclear HIPK2 localization and function by a SUMO interaction motif
2/2011, Biochimica et Biophysica Acta. Molecular Cell Research
Research Output: Contribution To Journal > Article

Autoregulatory control of the p53 response by Siah-1L-mediated HIPK2 degradation
3/2009, Biological Chemistry
Research Output: Contribution To Journal > Article

An inducible autoregulatory loop between HIPK2 and Siah2 at the apex of the hypoxic response
1/2009, Nature Cell Biology
Research Output: Contribution To Journal > Article

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