My research field covers the area of membrane-interacting proteins. For 31 years, I have studied the lipid regulation of membrane proteins such as Ca2+ -ATPase, the guanine nucleotide exchange factor SOS, the Ras protein, protein kinases C, insulin receptor, intermediate conductivity potassium channels, rabphilin 3A, SNAP-25, and synaptotagmin, among others. My lines of research, since my reincorporation in 1997 to the Biomembrane Group of the University of Murcia, have been focused on characterizing the structure and function of the family of protein kinases C; and how its regulatory domains interact with different types of membranes to decode a wide variety of signals in the cell. Many of our studies have represented a change in the classic paradigms of regulation and activation of these proteins. The resolution of the first 3D structure in 1999 revealed a new mechanism of interaction of the C2 domain of PKC with a membrane lipid-like phosphatidylserine and phosphoinositides. This has been an important insight in the field and has opened new avenues of research in the laboratory. In the medium and long term, our group continues to investigate the basic mechanisms of regulation of the activation of PKCs and other proteins such as rabphilin 3A and synaptotagmin. Our goal is to generate sufficient knowledge, at the molecular, genomic, and proteomic levels, to be able to design drugs and therapeutic strategies aimed at solving diseases such as cancer, or neurodegeneration.
My research field covers the area of membrane-interacting proteins. For 31 years, I have studied the lipid regulation of membrane proteins such as Ca2+ -ATPase, the guanine nucleotide exchange factor SOS, the Ras protein, protein kinases C, insulin receptor, intermediate conductivity potassium channels, rabphilin 3A, SNAP-25, and synaptotagmin, among others. My lines of research, since my reincorporation in 1997 to the Biomembrane Group of the University of Murcia, have been focused on characterizing the structure and function of the family of protein kinases C; and how its regulatory domains interact with different types of membranes to decode a wide variety of signals in the cell. Many of our studies have represented a change in the classic paradigms of regulation and activation of these proteins. The resolution of the first 3D structure in 1999 revealed a new mechanism of interaction of the C2 domain of PKC with a membrane lipid-like phosphatidylserine and phosphoinositides. This has been an important insight in the field and has opened new avenues of research in the laboratory. In the medium and long term, our group continues to investigate the basic mechanisms of regulation of the activation of PKCs and other proteins such as rabphilin 3A and synaptotagmin. Our goal is to generate sufficient knowledge, at the molecular, genomic, and proteomic levels, to be able to design drugs and therapeutic strategies aimed at solving diseases such as cancer, or neurodegeneration.