Summary of key activities carried out by the Programme

We over-expressed and purified several mg of the N-terminal domain of TBCC labelled with 13C and 15N, and the structure was solved at Dr. Rico´s lab.

We analyzed the human TBCB wild-type protein, their mutant derivatives Δ3 and Δ9, wild type TBCE and the Kenny-Caffey version of the protein, in Dr. Montoya´s lab by using several biophysical techniques as DLS, CD and fluorescence anisotropy.

We performed interaction studies of TBCE wt and TBCE Δ52-55 (Kenny-Caffey syndrome) with tubulin in vitro and in vivo.

We showed that TBCD is at centrosomes and the midbody, and is required for spindle organization, cell abscission, centriole formation and ciliogenesis. TBCD is the first centriolar protein identified that plays a role in the assembly of both, “centriolar rosettes” during early ciliogenesis, and at the procentriole budding site by S/G2. To study these processes we developed a new system model that allows the study of cilia development in primary cultures from mammalian ependymal cells. We also established a molecular link between the centriole and the midbody, demonstrating that this cofactor is also necessary for microtubule retraction during cell abscission. We completed structure/function analysis to determine the general regions of the protein that are involved in its localization.

We reported the first characterization of human TBCCD1 and showed that it is required for centrosome and Golgi apparatus perinuclear positioning in human cells. We also showed that TBCCD1 silenced cells are less efficient in primary cilia assembly and are affected in cell migration.

Web design: Alfonso Núñez Salgado