| Literature DB >> 16111475 |
Santiago Cavero1, Javier Traba, Araceli Del Arco, Jorgina Satrústegui.
Abstract
Sal1p is a mitochondrial protein that belongs to the SCaMC (short calcium-binding mitochondrial carrier) subfamily of mitochondrial carriers. The presence of calcium-binding motifs facing the extramitochondrial space allows the regulation of the transport activity of these carriers by cytosolic calcium and provides a new mechanism to transduce calcium signals in mitochondria without the requirement of calcium entry in the organelle. We have studied its transport activity, finding that it is a carboxyatractyloside-resistant ATP-Mg carrier. Mitochondria from a disruption mutant of SAL1 have a 50% reduction in the uptake of ATP. We have also found a clear stimulation of ATP-transport activity by calcium, with an S(0.5) of approx. 30 microM. Our results also suggest that Sal1p is a target of the glucose-induced calcium signal which is non-essential in wild-type cells, but becomes essential for transport of ATP into mitochondria in yeast lacking ADP/ATP translocases.Entities:
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Year: 2005 PMID: 16111475 PMCID: PMC1316293 DOI: 10.1042/BJ20050806
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857