Mitochondrial Kinases and the Role of Mitochondrial Protein Phosphorylation in Health and Disease

被引:22
作者
Kotrasova, Veronika [1 ]
Keresztesova, Barbora [1 ,2 ]
Ondrovicova, Gabriela [1 ]
Bauer, Jacob A. [1 ]
Havalova, Henrieta [1 ]
Pevala, Vladimir [1 ]
Kutejova, Eva [1 ]
Kunova, Nina [1 ,2 ]
机构
[1] Slovak Acad Sci, Inst Mol Biol, Dubravska Cesta 21, Bratislava 84551, Slovakia
[2] Charles Univ Prague, Inst Biol & Med Genet, Fac Med 1, Prague 12800, Czech Republic
来源
LIFE-BASEL | 2021年 / 11卷 / 02期
关键词
mitochondria; kinases; phosphorylation; disease;
D O I
10.3390/life11020082
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
The major role of mitochondria is to provide cells with energy, but no less important are their roles in responding to various stress factors and the metabolic changes and pathological processes that might occur inside and outside the cells. The post-translational modification of proteins is a fast and efficient way for cells to adapt to ever changing conditions. Phosphorylation is a post-translational modification that signals these changes and propagates these signals throughout the whole cell, but it also changes the structure, function and interaction of individual proteins. In this review, we summarize the influence of kinases, the proteins responsible for phosphorylation, on mitochondrial biogenesis under various cellular conditions. We focus on their role in keeping mitochondria fully functional in healthy cells and also on the changes in mitochondrial structure and function that occur in pathological processes arising from the phosphorylation of mitochondrial proteins.
引用
收藏
页码:1 / 37
页数:37
相关论文
共 385 条
[31]   Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism [J].
Bernstein, BE ;
Hol, WGJ .
BIOCHEMISTRY, 1998, 37 (13) :4429-4436
[32]  
Bhakar AL, 2003, J NEUROSCI, V23, P11373
[33]   Localization of LRRK2 to membranous and vesicular structures in mammalian brain [J].
Biskup, Saskia ;
Moore, Darren J. ;
Celsi, Fulvio ;
Higashi, Shinji ;
West, Andrew B. ;
Andrabi, Shaida A. ;
Kurkinen, Kaisa ;
Yu, Seong-Woon ;
Savitt, Joseph M. ;
Waldvogel, Henry J. ;
Faull, Richard L. M. ;
Emson, Piers C. ;
Torp, Reldun ;
Ottersen, Ole P. ;
Dawson, Ted M. ;
Dawson, Valina L. .
ANNALS OF NEUROLOGY, 2006, 60 (05) :557-569
[34]   The layered structure of human mitochondrial DNA nucleoids [J].
Bogenhagen, Daniel F. ;
Rousseau, Denis ;
Burke, Stephanie .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (06) :3665-3675
[35]  
BOLEN JB, 1987, ONCOGENE RES, V1, P149
[36]   SPERMINE-MEDIATED CASEIN KINASE II-UPTAKE BY RAT-LIVER MITOCHONDRIA [J].
BORDIN, L ;
CATTAPAN, F ;
CLARI, G ;
TONINELLO, A ;
SILIPRANDI, N ;
MORET, V .
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 1994, 1199 (03) :266-270
[37]   Rapid regulation of steroidogenesis by mitochondrial protein import [J].
Bose, HS ;
Lingappa, VR ;
Miller, WL .
NATURE, 2002, 417 (6884) :87-91
[38]   Evidence that pyruvate dehydrogenase kinase belongs to the ATPase/kinase superfamily [J].
Bowker-Kinley, M ;
Popov, KM .
BIOCHEMICAL JOURNAL, 1999, 344 :47-53
[39]   Evidence for existence of tissue-specific regulation of the mammalian pyruvate dehydrogenase complex [J].
Bowker-Kinley, MM ;
Davis, WI ;
Wu, PF ;
Harris, RA ;
Popov, KM .
BIOCHEMICAL JOURNAL, 1998, 329 :191-196
[40]   Posttranslational modification of Bcl-2 facilitates its proteasome-dependent degradation: Molecular characterization of the involved signaling pathway [J].
Breitschopf, K ;
Haendeler, J ;
Malchow, P ;
Zeiher, AM ;
Dimmeler, S .
MOLECULAR AND CELLULAR BIOLOGY, 2000, 20 (05) :1886-1896