María Lucas Gay (IP)

  • IBBTEC. C/ Albert Einstein 22, PCTCAN, 39011 Santander
  • maria.lucas@unican.es
  • 942 206 799 ext. 25921
  • Structural Biology of Macromolecular Complexes
  • Principal Investigator; Ramon y Cajal Researcher
  • Structural Biology
  • Department of Microbiology & Genomics

María Lucas obtained her MSc in Biochemistry from the University of the Basque Country (1999) and her PhD degree in Molecular Biology from the University of Cantabria (2006). She did her first postdoctoral work in CIC bioGUNE in the laboratory of Dr. Alfonso Martínez (2006-2008). Then, she continued her scientific career abroad in the laboratory of Dr. Karl-Peter Hopfner in the University of Munich LMU (2009-2012). To conduct this postdoctoral research she was awarded with a postdoctoral fellowship of the Basque Government. She returned to CIC bioGUNE in 2012, where she worked as a senior postdoctoral researcher for six years in the group of Dr. Aitor Hierro (2012-1017). In 2017 she was awarded with a Ramón y Cajal contract that has allowed her to join in 2018 the IBBTEC institute of the University of Cantabria as an independent investigator.

Her research activity is focused in the study of protein complexes by x-ray crystallography. Structural biology provides a precious atomic level knowledge that shows the molecular mechanisms of protein interactions and allows designing of drugs that modify, activate or inhibit proteins involved in pathological processes. She has worked in several fields with different protein families: nucleases involved in bacterial conjugation, oligomerization and regulatory modules, eukaryotic DNA break repair proteins, Legionella effector proteins and vesicular transport protein complexes involved in the recycling of transmembrane receptors. Nowadays, her main research line is the study of protein complexes involved in cellular trafficking related to neurodegenerative disorders. Her research group aims to elucidate the role of defects in endosomal trafficking in Alzheimer's disease. 


Structural Biology of Macromolecular Complexes



Research lines

    • Structure and function of protein complexes involved in intracellular vesicular traffic
    • Molecular and structural basis of neurodegenerative diseases
    • Structural basis of Host-Pathogen Interactions

Funding

Ramón y Cajal research award (2018-2021). Spanish Ministry of Economy and Competence (RYC-2016-20342). IP: María Lucas

CDC42EP5/BORG3 modulates SEPT9 to promote actomyosin function, migration, and invasion

CDC42EP5/BORG3 modulates SEPT9 to promote actomyosin function, migration, and invasion

Aaron J. Farrugia, Javier Rodríguez, Jose L. Orgaz, María Lucas, Victoria Sanz-Moreno, Fernando Calvo

​J Cell Biol (2020) 219 (9): e201912159. https://doi.org/10.1083/jcb.201912159. Epub 2020 Aug 14

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Identification of Relaxase-DNA Covalent Complexes and DNA Strand Transfer Reaction Products by Polyacrylamide Gel Electrophoresis.

Identification of Relaxase-DNA Covalent Complexes and DNA Strand Transfer Reaction Products by Polyacrylamide Gel Electrophoresis.

Lucas, M. and Moncalian, G.

Methods Mol Biol. 2075:145-156. doi: 10.1007/978-1-4939-9877-7

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Regulation of Human Hsc70 ATPase and Chaperone Activities by Apg2: Role of the Acidic Subdomain

Cabrera Y, Dublang L, Fernández-Higuero JA, Albesa-Jové D, Lucas M, Viguera AR, Guerin ME, Vilar JMG, Muga A, Moro F.

​J Mol Biol. 2019 Jan 18; 431(2):444-461. doi: 10.1016/j.jmb.2018.11.026. 

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RavN is a member of a previously unrecognized group of Legionella pneumophila E3 ubiquitin ligases.

Lin YH, Lucas M, Evans TR, Abascal-Palacios G, Doms AG, Beauchene NA, Rojas AL, Hierro A, Machner MP.

[PubMed]

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Molecular mechanism for the subversion of the retromer coat by the Legionella effector RidL.

Romano-Moreno M, Rojas AL, Williamson CD, Gershlick DC, Lucas M, Isupov MN, Bonifacino JS, Machner MP, Hierro A.Proc Natl Acad Sci U S A. 2017 Dec 26;114(52):E11151-E11160. doi:10.1073/pnas.1715361115

PubMed

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Endosomal Trafficking: Retromer and Retriever Are Relatives in Recycling.

Gershlick DC, Lucas M.

Curr Biol. 2017 Nov 20;27(22):R1233-R1236. 
doi: 10.1016/j.cub.2017.10.004 

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Retromer

Lucas M, Hierro A. Curr Biol. 2017 Jul 24; 27(14):687-689. doi: 10.1016/j.cub.2017.05.072

[PubMed]

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Structural Mechanism for Cargo Recognition by the Retromer Complex.

Lucas M, Gershlick DC, Vidaurrazaga A, Rojas AL, Bonifacino JS, Hierro A. Cell. 2016 Dec 1;167(6):1623-1635. doi: 10.1016/j.cell.2016.10.056

[PubMed]

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Structural basis for the recruitment and activation of the Legionella phospholipase VipD by the host GTPase Rab5.

Lucas M, Gaspar AH, Pallara C, Rojas AL, Fernández-Recio J, Machner MP, Hierro A. Proc Natl Acad Sci U S A. 2014, Aug 26; 111(34):E3514-23. doi: 10.1073/pnas.1405391111

[PubMed]

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The Mre11:Rad50 structure shows an ATP-dependent molecular clamp in DNA double-strand break repair.

Lammens K, Bemeleit DJ, Möckel C, Clausing E, Schele A, Hartung S, Schiller CB, Lucas M, Angermüller C, Söding J, Sträßer K, Hopfner KP. Cell. 2011 Apr1; 145(1):54-66. doi: 10.1016/j.cell.2011.02.038

[PubMed]

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Purification, crystallization and preliminary crystallographic analysis of the CBS domain protein MJ1004 from Methanocaldococcus jannaschii.

Oyenarte I, Lucas M, Gomez-García I, Martínez-Cruz LA. Acta Crystallogr Sect F, 2011 Mar 1; 67(3):318-24. doi: 10.1107/S1744309110053479

[PubMed]

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Relaxase DNA binding and cleavage are two distinguishable steps in conjugative DNA processing that involve different sequence elements of the nic site.

Lucas M, Gonzalez-Perez B, Cabezas M, Moncalián G, Rivas G, de la Cruz F. J Biol Chem. 2010 Mar 19; 285(12):8918-26. doi: 10.1074/jbc.M109.057539

[PubMed]

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Binding of S-Methyl-5'-Thioadenosine and S-Adenosyl-l-Methionine to Protein MJ0100 Triggers an Open-to-Closed Conformational Change in Its CBS Motif Pair.

Lucas M, Encinar JA, Arribas EA, Oyenarte I, García IG, Kortazar D, Fernández JA, Mato JM, Martínez-Chantar ML, Martínez-Cruz LA. J Mol Biol. 2010 feb 26; 396(3):800-20. doi: 10.1016/j.jmb.2009.12.012

[PubMed]

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The CBS domain protein MJ0729 of Methanocaldococcus jannaschii is a thermostable protein with a pH-dependent self-oligomerization.

Martínez-Cruz LA, Encinar JA, Kortazar D, Prieto J, Gómez J, Fernández-Millán P, Lucas M, Arribas EA, Fernández JA, Martínez-Chantar ML, Mato JM, Neira JL. Biochemistry. 2009 Mar 31; 48(12):2760-76. doi: 10.1021/bi801920r

[PubMed]

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Purification, crystallization and preliminary X-ray diffraction analysis of the CBS-domain pair from the Methanococcus jannaschii protein MJ0100.

Lucas M, Kortazar D, Astigarraga E, Fernández JA, Mato JM, Martínez-Chantar ML, Martínez-Cruz LA. Acta Crystallogr Sect F. 2008 Oct 1;64(10):936-41. doi: 10.1107/S1744309108027930

[PubMed]

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Crystallization and preliminary crystallographic analysis of merohedrally twinned crystals of MJ0729, a CBS-doman protein from Methanococcus jannaschii.

Fernández-Millán P, Kortazar D, Lucas M, Martínez-Chantar ML, Astigarraga-Arribas E, Fernández JA, Albert A, Mato JM, Martínez-Cruz LA. Acta Crystallogr Sect F. 2008 Jul 1;64(7):605-9. doi: 10.1107/S1744309108013432

[PubMed]

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Aurora Martín González

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Eva Martínez Lombardía

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