Contact:
gci@uaslp.mxThe calcium-activated
chloride channels play a role in numerous physiological processes such as:
water and electrolyte secretion, sensory transduction, regulation of vascular
tone, cardiac excitability and neuronal excitability. In 2008, the genes that
code for the proteins Anoctamine 1 or TMEM16A and Anoctamine 2 or TMEM16B were
cloned; these proteins form bona fide
calcium-activated chloride channels.
Our group has studied
the activation of Anoctamine-1 (TMEM16A) by calcium, voltage, chloride and
protons. In addition, we have used quantitative proteomics to identify 93
proteins associated with Anoctamine-1. Although we do not know the functional
relevance of most of these interactions, we have demonstrated that cytosolic
proteins such as Moesin and Calcineurin, and transmembrane proteins such as the
CFTR channel interact with Anoctamine-1 and modulate its activity. We are
currently studying how the function of TMEM16A channels depends on both the
proteins and the lipids that surround them.
Purinergic receptors
are cationic channels activated by extracellular ATP, which are expressed in
cells of the nervous system, immune system and other tissues. We have studied
the P2X4 and P2X7 receptors, both members of the P2X purinergic receptor
family. Although there are 7 members in this family, until 2007 it was believed
that P2X7 did not interact with other purinergic receptors. We showed that P2X4
and P2X7 indeed interact with each other through a protein-protein interaction.
This interaction is relevant for the physiological functions of mouse
macrophages. Also, we have documented the importance of P2X7 in the
phagocytosis of yeast and bacteria.