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Centro de Química e Bioquímica Telefone: +351 217500000 ext. 28239 |
Professor Coordenador da Escola Superior de Tecnologia da Saúde de Lisboa, Instituto Politécnico de Lisboa, Investigador do Centro de Química e Bioquímica (CQB) da Universidade de Lisboa
Habilitações Académicas
- Doutoramento em Ciências Biomédicas, Especialidade Biologia Molecular, disciplina afim Genética Molecular pelo Instituto de Ciências Biomédicas "Abel Salazar" da Universidade do Porto, 1992.
- Licenciatura em Biologia (ramo científico), pela Faculdade de Ciências da Universidade de Lisboa, 1986.
Actividade Docente /Teaching
Ver: http://www.estesl.ipl.pt/estesl/estrutura-organica/departamentos/ciencias-naturais-e-exatas/biologiaInteresses Científicos/Scientific interests
Os microtúbulos são polímeros polarizados de heterodímeros de α/β-tubulina que participam numa vasta variedade de funções celulares que vão da divisão celular, transporte intracelular, sinalização à locomoção. A via de folding da tubulina é um processo complexo que requer a interação da α- e β- tubulina com vários chaperones moleculares (e.g. the cytosolic chaperonin containing TCP1-CCT) e cofatores da tubulina (TBCA-TBCE).
Os estudos já desenvolvidos focaram-se de como os diferentes componentes da via de folding da tubulina podem constituir possíveis alvos para a regulação da dinâmica dos microtúbulos controlando a síntese o fluxo e o transporte da tubulina nativa.
Atualmente, estamos a estudar como a dinâmica dos microtúbulos está relacionada com as propriedades biofísicas destes polímeros, com o objetivo de estabelecer nano-devices onde os microtúbulos e as proteínas motoras a eles associadas podem ser usados como sistemas de entrega. Estamos também a investigar qual o papel do citoesqueleto de microtúbulos de parasitas pertencentes ao filo dos Apicomplexa na invasão celular do hospedeiro. Finalmente, temos como objetivo mostrar que o H2O2 possui um papel de regulador no centrossoma estando envolvido na regulação de processos celulares tão diversos como a dinâmica do citoesqueleto de microtúbulos e a biologia dos cílios, que têm impacto em patologias humanas, e.g. as doenças neurodegenerativas e envelhecimento. Neste contexto estamos a estudar a proteína TBCC-domain containing 1 (TBCCD1), que recentemente descrevemos como sendo uma possível proteína reguladora do posicionamento núcleo-centrossoma e, consequentemente, da organização interna da célula.
Microtubules (Mts) are polarized polymers of α/β-tubulin heterodimers participating in a wide range of cell functions, e.g. cell division, cell signaling, intracellular transport and locomotion. The maturation of tubulin heterodimers is a complex process involving the interaction of tubulins with several proteins: molecular chaperones (e.g. the cytosolic chaperonin containing TCP1-CCT) and the tubulin cofactors (TBCA-TBCE).
Our previous studies were focused in understanding how the components of the tubulin folding pathway control tubulin synthesis, flux, transport and heterodimers recycling and therefore are putative targets for regulation of the assembly of specialized microtubule structures like cilia and Mt dynamics.
We are now studying how microtubule dynamics in mammalian cells is related to the biophysical properties of these polymers, with the goal of establishing nano-devices where Mts and associated motor proteins are used as targeting systems. We are also investigating the critical role of the cross-talk between the microtubule cytoskeleton of the Apicomplexa protozoan parasites Besnoitia besnoiti and Toxoplasma gondii, and the microtubule cytoskeleton of the host cell in the event of host cell invasion. Finally, we are interested in uncovering a role for H2O2 as a key centrosomal regulatory molecule, involved in the regulation of a variety of cellular processes from microtubule cytoskeleton dynamics to cilia biology with impact in human diseases e.g neurodegenerative diseases and aging. In this context we are studying the TBCC-domain containing 1 (TBCCD1), which we described as being a putative key regulator of nucleus-centrosome positioning and, consequently, of internal cell organization.
Projectos em Curso / On-going Projects
- H2O2 uma molécula sinalizadora no centrossoma (PEst-OE/QUI/UI0612/2013)
- Member of the team of the project “The katanin role in Mt cytoskeleton remodeling during host cell invasion by Toxoplasma gondii” (FCT-PTDC/CVT/105470/2008) in collaboration with Sofia Nolasco (FMV)
- Member of the team of the project “Role of Mob1 and Unc119 proteins in cytokinesis and tumorogenesis” (PTDC/SAU-OBD/105234/2008) in collaboration with Álvaro Tavares (UALG)
Publicações Relevantes / Selected Publications
Soares H, Marinho HS, Real C, Antunes F. (2014) Cellular polarity in aging: role of redox regulation and nutrition. Genes Nutr 9(1):371.
Anita Quintal Gomes, Sofia Nolasco, Helena Soares (2013) Non-Coding RNAs: Multi-Tasking Molecules in the Cell. Int. J. Mol. Sci., 14, 16010-16039; doi:10.3390/ijms140816010; (Recommended in F1000; http://f1000.com/prime/718082667)
Carranza G, Castaño R, Fanarraga ML, Villegas JC, Gonçalves J, Soares H, Avila J, Marenchino M, Campos-Olivas R, Montoya G, Zabala JC. (2013) Autoinhibition of TBCB regulates EB1-mediated microtubule dynamics. Cell Mol Life Sci. 70 :357-71. (This paper was listed as a key scientific article in the edition of Global Medical Discovery Series; http://globalmedicaldiscovery.com/key-scientific-articles/autoinhibition-of-tbcb-regulates-eb1-mediated-microtubule-dynamics/.)
Nolasco S, Bellido J, Gonçalves J, Tavares A, Zabala JC, Soares H.(2012) The expression of tubulin cofactor A (TBCA) is regulated by a noncoding antisense Tbca RNA during testis maturation. PLoS One. 7(8):e42536. doi:10.1371/journal.pone.0042536.
Tavares A, Gonçalves J, Florindo C, Tavares AA, Soares H. (2012) Mob1: defining cell polarity for proper cell division. J Cell Sci. 125:516-27. (Paper chosen by Centro de Química e Bioquímica scientific advisory board as being the best CQB paper of 2012. Before this paper had been tagged as being of special interest to the drug development sector and was listed as a key scientific article in the edition of Global Medical Discovery Series.)
Gonçalves, J., Tavares, A, Carvalhal, S. and Soares, H. (2010) Revisiting the tubulin folding pathway: new roles in centrosomes and cilia. BioMol Concepts,1: 423–434
Seixas, AC., Cruto, T., Gaertig, J. and Soares, H. (2010) CCTα and CCTd chaperonin subunits are essential and required for cilia assembly and maintenance in Tetrahymena PLoS OneE 5(5): e10704. doi:10.1371/journal.pone.0010704.
Gonçalves, J, Nolasco,S, Nascimento, R, Lopez Fanarraga, M, Zabala, JC and Soares, H. (2010) TBCCD1, a new centrosomal protein is required for centrosome and Golgi apparatus positioning. EMBO Reports 11:194 – 200
Ramalho, R.R.,. Soares, H and Melo, L.V. (2007). Microtubule behavior under strong electromagnetic fields. Mat. Sci. Eng. C. 27:1207–1210.
Reis Y, Cortes H, Viseu Melo L, Fazendeiro I, Leitao A, Soares H. (2006) Microtubule cytoskeleton behavior in the initial steps of host cell invasion by Besnoitia besnoiti. FEBS Lett.580:4673-4682.
Nolasco, S., Bellido, J., Gonçalves, J., Zabala, JC and Soares, H. (2005) TBCA gene silencing in mammalian cells induces changes in microtubule cytoskeleton, cell cycle arrest and cell death.” FEBS Lett.579:3515-3524.
Casalou, C., Viseu Melo, L., Nolasco, S., Cecília Seixas, A., Brogueira, P. and Soares, H. (2003) "Subunits of the chaperonin CCT are associated with Tetrahymena microtubule structures and are involved in cilia biogenesis". Exp.Cell Res. 290:303-321.
Soares, H., Cyrne, L., Casalou, Ehmann, B. e Rodrigues-Pousada, C. (1997) "The third member of Tetrahymena CCT-subunit gene family, TpCCTα, encodes a component of the hetero-oligomeric chaperonin complex." Biochem J., 326: 21-29
Soares, H., Penque, D., Mouta, C. e Rodrigues-Pousada, C. (1994) "A Tetrahymena orthologue of the mouse chaperonin subunit CCTg and its co-expression with tubulin during cilia recovery" J. Biol. Chem., 269: 29299-29307.
Dujon, B., (...) Soares, H. (...) e Mewes, H.W. (Num total de 107 autores) (1994) "Complete DNA sequence of yeast chromosome XI" Nature, 369:371