Papa S, Scacco S, Sardanelli A M, Petruzzella V, Vergari R, Signorile A, Technikova-Dobrova Z
Department of Medical Biochemistry and Biology, University of Bari, Italy.
Biosci Rep. 2002 Feb;22(1):3-16. doi: 10.1023/a:1016004921277.
A cAMP-dependent protein kinase (PKA) is localized in mammalian mitochondria with the catalytic site at the matrix side of the membrane where it phosphorylates a number of proteins. One of these is the 18 kDa(IP) subunit of the mammalian complex I of the respiratory chain, encoded by the nuclear NDUFS4 gene. Mitochondria have a Ca(2+)-inhibited phosphatase, which dephosphorylates the 18 kDa phosphoprotein of complex I. In fibroblast and myoblast cultures cAMP-dependent phosphorylation of the 18 kDa protein is associated with stimulation of complex I and overall respiratory activity with NAD-linked substrates. Mutations in the human NDUFS4 gene have been found, which in the homozygous state are associated with deficiency of complex I and fatal neurological syndrome.
一种环磷酸腺苷（cAMP）依赖性蛋白激酶（PKA）定位于哺乳动物线粒体中，其催化位点位于膜的基质侧，在此它可使多种蛋白质磷酸化。其中之一是呼吸链哺乳动物复合物I的18 kDa（IP）亚基，由核基因NDUFS4编码。线粒体有一种钙抑制磷酸酶，可使复合物I的18 kDa磷蛋白去磷酸化。在成纤维细胞和成肌细胞培养物中，18 kDa蛋白的cAMP依赖性磷酸化与复合物I的刺激以及与NAD相关底物的整体呼吸活性相关。已发现人类NDUFS4基因中的突变，纯合状态下这些突变与复合物I缺乏和致命性神经综合征相关。
