Letizia Albarrán

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Canonical transient receptor potential-1 (TRPC1) is an almost ubiquitously expressed channel that plays a relevant role in cell function. As other TRPC members, TRPC1 forms receptor-operated cation channels that exhibit both STIM1-dependent and store-independent behaviour. The STIM1 inhibitor SARAF (for store-operated Ca(2+) entry (SOCE)-associated(More)
Three decades ago, store-operated Ca(2+) entry (SOCE) was identified as a unique mechanism for Ca(2+) entry through plasma membrane (PM) Ca(2+)-permeable channels modulated by the intracellular Ca(2+) stores, mainly the endoplasmic reticulum (ER). Extensive analysis of the communication between the ER and the PM leads to the identification of the protein(More)
Calcium influx is an essential mechanism for the activation of cellular functions both in excitable and non-excitable cells. In non-excitable cells, activation of phospholipase C by occupation of G protein-coupled receptors leads to the generation of inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG), which, in turn, initiate two Ca(2+) entry(More)
Ca(2+) influx by store-operated Ca(2+) channels is a major mechanism for intracellular Ca(2+) homeostasis and cellular function. Here we present evidence for the dynamic interaction between the SOCE-associated regulatory factor (SARAF), STIM1 and Orai1. SARAF overexpression attenuated SOCE and the STIM1-Orai1 interaction in cells endogenously expressing(More)
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