Cell cycle–dependent regulation of mitochondrial preprotein translocase

Science ◽  
2014 ◽  
Vol 346 (6213) ◽  
pp. 1109-1113 ◽  
Author(s):  
Angelika B. Harbauer ◽  
Magdalena Opalińska ◽  
Carolin Gerbeth ◽  
Josip S. Herman ◽  
Sanjana Rao ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Protein Import ◽  
Respiratory Activity ◽  
Mitochondrial Protein ◽  
Cyclin Dependent Kinase ◽  
Mitochondrial Protein Import ◽  
Cellular Energy ◽  
Specific Manner ◽  
A Cell ◽  
Cycle Dependent

Mitochondria play central roles in cellular energy conversion, metabolism, and apoptosis. Mitochondria import more than 1000 different proteins from the cytosol. It is unknown if the mitochondrial protein import machinery is connected to the cell division cycle. We found that the cyclin-dependent kinase Cdk1 stimulated assembly of the main mitochondrial entry gate, the translocase of the outer membrane (TOM), in mitosis. The molecular mechanism involved phosphorylation of the cytosolic precursor of Tom6 by cyclin Clb3-activated Cdk1, leading to enhanced import of Tom6 into mitochondria. Tom6 phosphorylation promoted assembly of the protein import channel Tom40 and import of fusion proteins, thus stimulating the respiratory activity of mitochondria in mitosis. Tom6 phosphorylation provides a direct means for regulating mitochondrial biogenesis and activity in a cell cycle-specific manner.

Importin α/β-mediated nuclear protein import is regulated in a cell cycle-dependent manner

2004 ◽  
Vol 297 (1) ◽  
pp. 285-293 ◽  
Author(s):  
Noriko Yasuhara ◽  
Eri Takeda ◽  
Hitomi Inoue ◽  
Ippei Kotera ◽  
Yoshihiro Yoneda
Keyword(s):  
Cell Cycle ◽  
Protein Import ◽  
Nuclear Protein ◽  
Dependent Manner ◽  
Importin Α ◽  
A Cell ◽  
Nuclear Protein Import ◽  
Cycle Dependent

The plant homologue of MAP kinase is expressed in a cell cycle-dependent and organ-specific manner

1993 ◽  
Vol 3 (4) ◽  
pp. 611-617 ◽  
Author(s):  
Claudia Jonak ◽  
Aniko Páy ◽  
Laszlo Börge ◽  
Heribert Hirt ◽  
Erwin Heberle-Bors
Keyword(s):  
Cell Cycle ◽  
Map Kinase ◽  
Specific Manner ◽  
Organ Specific ◽  
A Cell ◽  
Cycle Dependent ◽  
Plant Homologue

scholarly journals Cell cycle regulation of mitochondrial protein import revealed by genome-scale pooled bimolecular fluorescence complementation screening

2019 ◽  
Author(s):  
Kim Blakely ◽  
Patricia Mero ◽  
Roland Arnold ◽  
Ayesha Saleem ◽  
Christine Misquitta ◽  
...  
Keyword(s):  
Cell Cycle ◽  
High Throughput ◽  
Protein Interactions ◽  
Protein Import ◽  
Mitochondrial Protein ◽  
Protein Protein Interactions ◽  
Mitochondrial Protein Import ◽  
Interaction Partners ◽  
Genome Scale ◽  
Bimolecular Fluorescence

ABSTRACTA central focus of systems biology is the functional mapping of protein-protein interactions under physiological conditions. Here we describe MaGiCaL-BiFC, a lentivirus-based bimolecular fluorescence protein-fragment complementation approach for the high-throughput, genome-scale identification of protein-protein interactions in mammalian cells. After developing and validating this methodology using known protein-protein interaction pairs, we constructed genome-scale pooled BiFC libraries using the human ORFeome cDNA collection. These pooled libraries, containing ∼ 12,000 unique human cDNAs, were used to screen for candidate interaction partners of the mitochondrial transmembrane protein TOMM22. Following infection of cells with the TOMM22 bait and the pooled cDNA libraries, cells harboring candidate TOMM22 interacting proteins were isolated from the cell pool via fluorescence activated cell sorting, and identified via microarray analysis. This approach identified several known interaction partners of TOMM22, as well as novel physical and functional partners that link the mitochondrial network to proteins involved in diverse cellular processes. Notably, protein kinase CK2 was identified as a novel physical interaction partner of human TOMM22. We found that this association occurs preferentially during mitosis and involves direct phosphorylation of TOMM22, an event that may lead to attenuation of mitochondrial protein import. Together, this data contributes to the growing body of evidence suggesting eloquent coordination between cell cycle progression and mitochondrial physiology. Importantly, through high-throughput screening and focused validation, our study demonstrates the power of the MaGiCaL-BiFC approach to uncover novel functional protein-protein interactions, including those involving proteins with membrane-spanning domains, or of a transient nature, all within their native cellular environment.

A mutation in the yeast heat-shock factor gene causes temperature-sensitive defects in both mitochondrial protein import and the cell cycle

1991 ◽  
Vol 11 (5) ◽  
pp. 2647-2655 ◽  
Author(s):  
B J Smith ◽  
M P Yaffe
Keyword(s):  
Cell Cycle ◽  
Heat Shock ◽  
Cell Cycle Progression ◽  
Protein Import ◽  
Mitochondrial Protein ◽  
Yeast Cells ◽  
Heat Shock Gene ◽  
Temperature Sensitive ◽  
Mitochondrial Protein Import ◽  
Cycle Progression

Yeast cells containing the recessive mas3 mutation display temperature-sensitive defects in both mitochondrial protein import and the cell division cycle. The import defect is characterized by two pools of mitochondrial precursors and a dramatically slower rate of posttranslational import. The effect of mas3 on cell cycle progression occurs within one cell cycle at the nonpermissive temperature and retards progression through the G2 stage. The mas3 mutation maps to the gene encoding yeast heat-shock transcription factor (HSF), and expression of wild-type HSF complements the temperature-sensitive defects. The mas3 lesion has no apparent effect on protein secretion. In mas3 cells, induction of a major heat-shock gene, SSA1, is defective at 37 degrees C. The properties of the mas3 mutant cells indicate that HSF mediates the response to stress of two basic cellular processes: mitochondrial protein import and cell cycle progression.

scholarly journals A mutation in the yeast heat-shock factor gene causes temperature-sensitive defects in both mitochondrial protein import and the cell cycle.

1991 ◽  
Vol 11 (5) ◽  
pp. 2647-2655 ◽  
Author(s):  
B J Smith ◽  
M P Yaffe
Keyword(s):  
Cell Cycle ◽  
Heat Shock ◽  
Cell Cycle Progression ◽  
Protein Import ◽  
Mitochondrial Protein ◽  
Yeast Cells ◽  
Heat Shock Gene ◽  
Temperature Sensitive ◽  
Mitochondrial Protein Import ◽  
Cycle Progression

Yeast cells containing the recessive mas3 mutation display temperature-sensitive defects in both mitochondrial protein import and the cell division cycle. The import defect is characterized by two pools of mitochondrial precursors and a dramatically slower rate of posttranslational import. The effect of mas3 on cell cycle progression occurs within one cell cycle at the nonpermissive temperature and retards progression through the G2 stage. The mas3 mutation maps to the gene encoding yeast heat-shock transcription factor (HSF), and expression of wild-type HSF complements the temperature-sensitive defects. The mas3 lesion has no apparent effect on protein secretion. In mas3 cells, induction of a major heat-shock gene, SSA1, is defective at 37 degrees C. The properties of the mas3 mutant cells indicate that HSF mediates the response to stress of two basic cellular processes: mitochondrial protein import and cell cycle progression.

scholarly journals NSun2 Promotes Cell Growth via Elevating Cyclin-Dependent Kinase 1 Translation

2015 ◽  
Vol 35 (23) ◽  
pp. 4043-4052 ◽  
Author(s):  
Junyue Xing ◽  
Jie Yi ◽  
Xiaoyu Cai ◽  
Hao Tang ◽  
Zhenyun Liu ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Cell Division ◽  
Cell Division Cycle ◽  
Mrna Levels ◽  
Dependent Manner ◽  
Cyclin Dependent Kinase ◽  
A Cell ◽  
Cycle Dependent ◽  
Insight Into

The tRNA methytransferase NSun2 promotes cell proliferation, but the molecular mechanism has not been elucidated. Here, we report that NSun2 regulates cyclin-dependent kinase 1 (CDK1) expression in a cell cycle-dependent manner. Knockdown of NSun2 decreased the CDK1 protein level, while overexpression of NSun2 elevated it without alteringCDK1mRNA levels. Further studies revealed that NSun2 methylatedCDK1mRNAin vitroand in cells and that methylation by NSun2 enhanced CDK1 translation. Importantly, NSun2-mediated regulation of CDK1 expression had an impact on the cell division cycle. These results provide new insight into the regulation of CDK1 during the cell division cycle.

Sign in / Sign up

Export Citation Format

Share Document