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Research Group
Molecular mechanisms in neurosecretion
Unit Unit Molecular Neurobiology »

Principal Investigator Graduate students Technician
Research Fields
Molecular mechanisms of exocytosis in a neuroendocrine model: the involvement of cytoskeleton and SNARE complex proteins
Adrenomedullary chromaffin cells have been used as an excellent experimental model to study the exocytosis and therefore the molecular mechanisms of neurotransmission. It is now clear that the proteins involved in the processes of vesicle docking, membrane fusion and neurotransmitter release are common to many cellular systems (SNARE hypothesis). Our research interest is focused in two different aspects of the molecular mechanisms of neurotransmission: Implication of molecular motors such myosin-actin in vesicle transport during neurosecretion and the determination of essential aminoacids of synaptobrevin or SNAP-25 implicated in the process of membrane fusion. Experimental approaches involve strategies using antibodies, sequence peptide design and protein overexpression that demonstrate the participation of specific protein domains in exocytosis. In addition, the role of these proteins on the secretory stages have been studied using amperometry, technique that resolves single fusion events.


Representative Publications

Criado, M. , Gil, A., Viniegra, S., Gutiérrez, L.M. " A single amino acid near the C-terminus of the synaptosome-associated protein-25 (SNAP-25) is essential for exocytosis in chromaffin cells. " Proc. Natl. Acad. Sci. . 96 , 7256 - 7261 ( 1999 )

Gil, A. , Rueda, J., Viniegra, S., Gutierrez, L.M. " The f-actin cytoskeleton modulates slow secretory components rather than readily releasable pools in bovine chromaffin cells. " Neuroscience. . 98 , 605 - 614 ( 2000 )

Gil, A. , Gutiérrez, L.M., Carrasco-Serrano, M.C., Alonso, T., Viniegra, S., and Criado, M. " Modifications in the C-terminus of the synaptosome-associated protein of 25 kDa (SNAP-25) and in the complementary region of synaptobrevin affect the final steps of exocytosis. " J. Biol. Chem. . 277 , 9904 - 9910 ( 2002 )

Ñeco, P. , Rosetto, O, Gil, A., Montecucco, C., and Gutiérrez, L.M. " Taipoxin induces F-actin fragmentation and enhances release of catecholamines in bovine chromaffin cells " J. Neurochem . 85 , 329 - 337 ( 2003 )

Ñeco, P. , Giner, D., Francés, M.M., Viniegra, S., and Gutiérrez, L.M. " Differential participation of Actin and Tubulin-based Vesicle Transport Systems during Secretion in Bovine Chromaffin Cells " Eur. J. Neurosci. . 18 , 733 - 742 ( 2003 )
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Universidad Miguel Hernández

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