Responsable: Manuel Muñiz Guinea
Tipo de Proyecto/Ayuda: Plan Nacional del 2008
Referencia: BFU2008-04119
Fecha de Inicio: 01-01-2009
Fecha de Finalización: 31-12-2011

Empresa/Organismo financiador/es:

• Ministerio de Ciencia e Innovación

Equipo:

• Otros Investigadores:
  • María Auxiliadora Aguilera Romero

Contratados:

• Investigadores:
  • María Auxiliadora Aguilera Romero
  • Javier Manzano López
• Técnicos/Personal Administrativo:
  • María Auxiliadora Aguilera Romero

Resumen del proyecto:

In eukaryotic cells, protein transport between the organelles of the secretory pathway is mediated by vesicles that bud from a donor compartment and fuse with an appropriate acceptor compartment. Cytoplasmic coat proteins are known to sculpt vesicles by locally deforming the donor membrane. In addition to the coat components, it has been proposed that some transmembrane cargo proteins might be also important for vesicle formation instead of simply being a passive traveller. The p24 transmembrane proteins are assembled into heteromeric complexes that continuously cycle between ER and Golgi compartments. Our results suggest that p24 proteins might be required for the budding process by acting as a primer to induce coat polimerization. Additionally, p24 proteins might also function as a cargo receptor by the recruitment of specific proteins into the vesicles. The aim of this proposal is to analyse the role played by the p24 complex in vesicle formation during bidirectional transport between ER and Golgi using the yeast Saccharomyces cerevisiae as a cell-model system. We will address the role of the p24 complex in these processes: 1) The formation of COPI-coated vesicles from the Golgi. 2) The sorting of GPI-anchored proteins upon ER exit. It is our hope that this study will allow us to better understand the operation of vesicle biogenesis mechanisms at the early secretory pathway.