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Activation of a TRP-like channel and intracellular Ca2+ dynamics during phospholipase-C-mediated cell death.


ABSTRACT: The model organism Neurospora crassa undergoes programmed cell death when exposed to staurosporine. Here, we show that staurosporine causes defined changes in cytosolic free Ca(2+) ([Ca(2+)]c) dynamics and a distinct Ca(2+) signature that involves Ca(2+) influx from the external medium and internal Ca(2+) stores. We investigated the molecular basis of this Ca(2+) response by using [Ca(2+)]c measurements combined with pharmacological and genetic approaches. Phospholipase C was identified as a pivotal player during cell death, because modulation of the phospholipase C signaling pathway and deletion of PLC-2, which we show to be involved in hyphal development, results in an inability to trigger the characteristic staurosporine-induced Ca(2+) signature. Using ?cch-1, ?fig-1 and ?yvc-1 mutants and a range of inhibitors, we show that extracellular Ca(2+) entry does not occur through the hitherto described high- and low-affinity Ca(2+) uptake systems, but through the opening of plasma membrane channels with properties resembling the transient receptor potential (TRP) family. Partial blockage of the response to staurosporine after inhibition of a putative inositol-1,4,5-trisphosphate (IP3) receptor suggests that Ca(2+) release from internal stores following IP3 formation combines with the extracellular Ca(2+) influx.

SUBMITTER: Goncalves AP 

PROVIDER: S-EPMC4150065 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature

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Activation of a TRP-like channel and intracellular Ca2+ dynamics during phospholipase-C-mediated cell death.

Gonçalves A Pedro AP   Cordeiro J Miguel JM   Monteiro João J   Muñoz Alberto A   Correia-de-Sá Paulo P   Read Nick D ND   Videira Arnaldo A  

Journal of cell science 20140718 Pt 17


The model organism Neurospora crassa undergoes programmed cell death when exposed to staurosporine. Here, we show that staurosporine causes defined changes in cytosolic free Ca(2+) ([Ca(2+)]c) dynamics and a distinct Ca(2+) signature that involves Ca(2+) influx from the external medium and internal Ca(2+) stores. We investigated the molecular basis of this Ca(2+) response by using [Ca(2+)]c measurements combined with pharmacological and genetic approaches. Phospholipase C was identified as a piv  ...[more]

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