Extranuclear Localization of SIRT1 and PGC-1α: An Insight into Possible Roles in Diseases Associated with Mitochondrial Dysfunction

被引:60
作者
Aquilano, K. [1 ]
Baldelli, S. [1 ]
Pagliei, B. [1 ]
Ciriolo, M. R. [1 ,2 ]
机构
[1] Univ Roma Tor Vergata, Dept Biol, I-00133 Rome, Italy
[2] IRCCS San Raffaele, Res Ctr, I-00166 Rome, Italy
关键词
Biogenesis; cellular metabolism; cytoplasm; mitochondria; mitochondrial diseases; transcriptional regulation; AMYOTROPHIC-LATERAL-SCLEROSIS; TRANSCRIPTIONAL COACTIVATOR PGC-1-ALPHA; FATTY-ACID OXIDATION; SKELETAL-MUSCLE; ADP-RIBOSYLTRANSFERASE; CALORIE RESTRICTION; ENERGY-EXPENDITURE; PARKINSONS-DISEASE; LYSINE ACETYLATION; DEACETYLASE SIRT1;
D O I
10.2174/156652413804486241
中图分类号
R-3 [医学研究方法]; R3 [基础医学];
学科分类号
1001 ;
摘要
SIRT1 and PGC-1 alpha are two nutrient sensing master regulators of cellular metabolism and their up-regulation is often linked to increased lifespan. SIRT1 and PGC-1 alpha modulate the expression of a set of nuclear genes controlling many metabolic pathways. In recent years mounting evidence has indicated the implication of these proteins in several mitochondrial diseases including neurodegenerative disorders, myopathies and Type II diabetes mellitus. Recently, these proteins have been localized in cytoplasm and mitochondria wherein they target novel substrates opening new insight into their possible function in modulating extranuclear genes and proteins. This review will firstly summarize the nuclear function of SIRT1 and PGC-1 alpha. Then, data from papers demonstrating the presence of SIRT1 and PGC-1 alpha in the cytoplasm and in mitochondria will be outlined so that these extranuclear forms do not remain out of sight. Finally, very recent evidence of the alteration of the pathways governed by SIRT1 and PGC-1 alpha in human mitochondrial diseases will be described and the possible role of their mitochondrial forms will be briefly discussed.
引用
收藏
页码:140 / 154
页数:15
相关论文
共 136 条
[1]   Mitochondrial DNA damage is a hallmark of chemically induced and the R6/2 transgenic model of Huntington's disease [J].
Acevedo-Torres, Karina ;
Berrios, Lexsy ;
Rosario, Nydia ;
Dufault, Vanessa ;
Skatchkov, Serguei ;
Eaton, Misty J. ;
Torres-Ramos, Carlos A. ;
Ayala-Torres, Sylvette .
DNA REPAIR, 2009, 8 (01) :126-136
[2]   A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis [J].
Ahn, Bong-Hyun ;
Kim, Hyun-Seok ;
Song, Shiwei ;
Lee, In Hye ;
Liu, Jie ;
Vassilopoulos, Athanassios ;
Deng, Chu-Xia ;
Finkel, Toren .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2008, 105 (38) :14447-14452
[3]   Regulation of insulin secretion by SIRT4, a mitochondrial ADP-ribosyltransferase [J].
Ahuja, Nidhi ;
Schwer, Bjoern ;
Carobbio, Stefania ;
Waltregny, David ;
North, Brian J. ;
Castronovo, Vincenzo ;
Maechler, Pierre ;
Verdin, Eric .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (46) :33583-33592
[4]   Sirtuins as Novel Targets for Alzheimer's Disease and Other Neurodegenerative Disorders: Experimental and Genetic Evidence [J].
Albani, Diego ;
Polito, Letizia ;
Forloni, Gianluigi .
JOURNAL OF ALZHEIMERS DISEASE, 2010, 19 (01) :11-26
[5]   The SIRT1 activator resveratrol protects SK-N-BE cells from oxidative stress and against toxicity caused by α-synuclein or amyloid-β (1-42) peptide [J].
Albani, Diego ;
Polito, Letizia ;
Batelli, Sara ;
De Mauro, Stefania ;
Fracasso, Claudia ;
Martelli, Giuliana ;
Colombo, Laura ;
Manzoni, Claudia ;
Salmona, Mario ;
Caccia, Silvio ;
Negro, Alessandro ;
Forloni, Gianluigi .
JOURNAL OF NEUROCHEMISTRY, 2009, 110 (05) :1445-1456
[6]   A Biotin Switch-Based Proteomics Approach Identifies 14-3-3ζ as a Target of Sirt1 in the Metabolic Regulation of Caspase-2 [J].
Andersen, Joshua L. ;
Thompson, J. Will ;
Lindblom, Kelly R. ;
Johnson, Erika S. ;
Yang, Chih-Sheng ;
Lilley, Lauren R. ;
Freel, Christopher D. ;
Moseley, M. Arthur ;
Kornbluth, Sally .
MOLECULAR CELL, 2011, 43 (05) :834-842
[7]   Dynamic regulation of PGC-1α localization and turnover implicates mitochondrial adaptation in calorie restriction and the stress response [J].
Anderson, Rozalyn M. ;
Barger, Jamie L. ;
Edwards, Michael G. ;
Braun, Kristina H. ;
O'Connor, Clare E. ;
Prolla, Tomas A. ;
Weindruch, Richard .
AGING CELL, 2008, 7 (01) :101-111
[8]   Peroxisome Proliferator-activated Receptor γ Co-activator 1α (PGC-1α) and Sirtuin 1 (SIRT1) Reside in Mitochondria POSSIBLE DIRECT FUNCTION IN MITOCHONDRIAL BIOGENESIS [J].
Aquilano, Katia ;
Vigilanza, Paola ;
Baldelli, Sara ;
Pagliei, Beatrice ;
Rotilio, Giuseppe ;
Ciriolo, Maria Rosa .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2010, 285 (28) :21590-21599
[9]   Resveratrol is Not a Direct Activator of SIRT1 Enzyme Activity [J].
Beher, Dirk ;
Wu, John ;
Cumine, Suzanne ;
Kim, Ki Won ;
Lu, Shu-Chen ;
Atangan, Larissa ;
Wang, Minghan .
CHEMICAL BIOLOGY & DRUG DESIGN, 2009, 74 (06) :619-624
[10]   The sirtuin pathway in ageing and Alzheimer disease: mechanistic and therapeutic considerations [J].
Bonda, David J. ;
Lee, Hyoung-gon ;
Camins, Antoni ;
Pallas, Merce ;
Casadesus, Gemma ;
Smith, Mark A. ;
Zhu, Xiongwei .
LANCET NEUROLOGY, 2011, 10 (03) :275-279