The calcium-dependent ATP-Mg/Pi mitochondrial carrier is a target of glucose-induced calcium signalling in Saccharomyces cerevisiae

被引:46
作者
Cavero, S
Traba, J
Del Arco, A
Satrústegui, J
机构
[1] Univ Autonoma Madrid, Fac Ciencias, CSIC,Dept Biol Mol, Ctr Biol Mol Severo Ochoa, E-28049 Madrid, Spain
[2] Univ Castilla La Mancha, Fac Cienias Medio Ambiente, Area Bioquim, CRIB, Toledo 45071, Spain
关键词
ATP transport; calcium; calcium-dependent mitochondrial carrier (CaMC); glucose-sensing; short calcium-binding mitochondrial carrier (SCaMC); Saccharomyces cerevisiae;
D O I
10.1042/BJ20050806
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
found a clear stimulation of ATP-transport activity by calcium, with an SO 5 of approx. 30 [mu M. Our results also suggest that Sal 1p is a target of the glucose-induced calcium signal which is nonessential in wild-type cells, but becomes essential for transport of ATP into mitochondria in yeast lacking ADP/ATP translocases.Sallp 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-05 of approx. 30 mu M. Our results also suggest that Sal 1p is a target of the glucose-induced calcium signal which is nonessential in wild-type cells, but becomes essential for transport of ATP into mitochondria in yeast lacking ADP/ATP translocases.
引用
收藏
页码:537 / 544
页数:8
相关论文
共 39 条
[1]   Phospholipase C binds to the receptor-like GPR1 protein and controls pseudohyphal differentiation in Saccharomyces cerevisiae [J].
Ansari, K ;
Martin, S ;
Farkasovsky, M ;
Ehbrecht, IM ;
Küntzel, H .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (42) :30052-30058
[2]   REGULATION OF THE MITOCHONDRIAL ADENINE-NUCLEOTIDE POOL SIZE [J].
APRILLE, JR ;
AUSTIN, J .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1981, 212 (02) :689-699
[4]   CYSTEINE RESIDUES ARE NOT ESSENTIAL FOR UNCOUPLING PROTEIN FUNCTION [J].
ARECHAGA, I ;
RAIMBAULT, S ;
PRIETO, S ;
LEVIMEYRUEIS, C ;
ZARAGOZA, P ;
MIROUX, B ;
RICQUIER, D ;
BOUILLAUD, F ;
RIAL, E .
BIOCHEMICAL JOURNAL, 1993, 296 :693-700
[7]   SURVEY OF INTERACTION OF CALCIUM IONS WITH MITOCHONDRIA FROM DIFFERENT TISSUES AND SPECIES [J].
CARAFOLI, E ;
LEHNINGE.AL .
BIOCHEMICAL JOURNAL, 1971, 122 (05) :681-&
[8]   Identification and metabolic role of the mitochondrial aspartate-glutamate transporter in Saccharomyces cerevisiae [J].
Cavero, S ;
Vozza, A ;
del Arco, A ;
Palmieri, L ;
Villa, A ;
Blanco, E ;
Runswick, MJ ;
Walker, JE ;
Cerdán, S ;
Palmieri, F ;
Satrústegui, J .
MOLECULAR MICROBIOLOGY, 2003, 50 (04) :1257-1269
[9]   Sallp, a calcium-dependent cartier protein that suppresses an essential cellular function associated with the Aac2 isoform of ADP/ATP translocase in Saccharomyces cerevisiae [J].
Chen, XJ .
GENETICS, 2004, 167 (02) :607-617
[10]   Vps10p cycles between the late-Golgi and prevacuolar compartments in its function as the sorting receptor for multiple yeast vacuolar hydrolases [J].
Cooper, AA ;
Stevens, TH .
JOURNAL OF CELL BIOLOGY, 1996, 133 (03) :529-541