scholarly journals Involvement of DNA-dependent Protein Kinase in Normal Cell Cycle Progression through Mitosis

2011 ◽  
Vol 286 (14) ◽  
pp. 12796-12802 ◽  
Author(s):  
Kyung-Jong Lee ◽  
Yu-Fen Lin ◽  
Han-Yi Chou ◽  
Hirohiko Yajima ◽  
Kazi R. Fattah ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Protein Kinase ◽  
Normal Cell ◽  
Cell Cycle Progression ◽  
Dependent Protein Kinase ◽  
Cycle Progression ◽  
Dependent Protein ◽  
Normal Cell Cycle

scholarly journals The Localization and Activity of cAMP-dependent Protein Kinase Affect Cell Cycle Progression in Thyroid Cells

2000 ◽  
Vol 275 (1) ◽  
pp. 303-311 ◽  
Author(s):  
Antonio Feliciello ◽  
Adriana Gallo ◽  
Evelina Mele ◽  
Antonio Porcellini ◽  
Giancarlo Troncone ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Protein Kinase ◽  
Cell Cycle Progression ◽  
Dependent Protein Kinase ◽  
Thyroid Cells ◽  
Cycle Progression ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein ◽  
Affect Cell Cycle Progression

Involvement of DNA-dependent protein kinase in down-regulation of cell cycle progression

2003 ◽  
Vol 35 (4) ◽  
pp. 432-440 ◽  
Author(s):  
Fumiaki Watanabe ◽  
Ken-ichi Shinohara ◽  
Hirobumi Teraoka ◽  
Kenshi Komatsu ◽  
Kouichi Tatsumi ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Protein Kinase ◽  
Cell Cycle Progression ◽  
Down Regulation ◽  
Dependent Protein Kinase ◽  
Cycle Progression ◽  
Dependent Protein ◽  
Regulation Of Cell Cycle

Calmodulin-dependent protein kinase II is required for G1/S progression in HeLa cells

1995 ◽  
Vol 73 (3-4) ◽  
pp. 201-207 ◽  
Author(s):  
Grace Rasmussen ◽  
Colin Rasmussen
Keyword(s):  
Cell Cycle ◽  
Protein Kinase ◽  
Dna Synthesis ◽  
Hela Cells ◽  
Cell Cycle Progression ◽  
Dependent Protein Kinase ◽  
Cycle Progression ◽  
Cycle Arrest ◽  
Calmodulin Kinase ◽  
Dependent Protein

Calmodulin (CaM) has been previously shown to be essential for cell cycle progression in eukaryotic cells, being required at the G1/S,G2/M, and metaphase–anaphase transitions. Little is known about the specific CaM-dependent enzymes that mediate Ca2+/CaM signaling to affect cell proliferation. In this study we show that inhibition of calmodulin kinase II (CaMKII) in HeLa cells using the CaMKII inhibitor KN-93 causes cell cycle arrest, demonstrating that CaMKII is required for cell cycle progression. Detailed analysis of arrest cells suggests that CaMKII is required for the initiation of DNA synthesis. Cells treated with KN-93 arrest with a G1 DNA content, but with elevated cyclin-dependent histone H1 kinase activity, suggesting that CaMKII may act at a point very close to the onset of DNA synthesis in mammalian cells.Key words: calmodulin, protein kinase, cell cycle, HeLa.

scholarly journals Chk1-mediated Cdc25A degradation as a critical mechanism for normal cell cycle progression

2019 ◽  
Vol 132 (2) ◽  
pp. jcs223123 ◽  
Author(s):  
Hidemasa Goto ◽  
Toyoaki Natsume ◽  
Masato T. Kanemaki ◽  
Aika Kaito ◽  
Shujie Wang ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Normal Cell ◽  
Cell Cycle Progression ◽  
Cycle Progression ◽  
Normal Cell Cycle

scholarly journals The decision to enter mitosis: feedback and redundancy in the mitotic entry network

2009 ◽  
Vol 185 (2) ◽  
pp. 193-202 ◽  
Author(s):  
Arne Lindqvist ◽  
Verónica Rodríguez-Bravo ◽  
René H. Medema
Keyword(s):  
Cell Cycle ◽  
Normal Cell ◽  
Cell Cycle Progression ◽  
Feedback Loops ◽  
Cyclin B ◽  
Cycle Progression ◽  
Mitotic Entry ◽  
Different Levels ◽  
Normal Cell Cycle

The decision to enter mitosis is mediated by a network of proteins that regulate activation of the cyclin B–Cdk1 complex. Within this network, several positive feedback loops can amplify cyclin B–Cdk1 activation to ensure complete commitment to a mitotic state once the decision to enter mitosis has been made. However, evidence is accumulating that several components of the feedback loops are redundant for cyclin B–Cdk1 activation during normal cell division. Nonetheless, defined feedback loops become essential to promote mitotic entry when normal cell cycle progression is perturbed. Recent data has demonstrated that at least three Plk1-dependent feedback loops exist that enhance cyclin B–Cdk1 activation at different levels. In this review, we discuss the role of various feedback loops that regulate cyclin B–Cdk1 activation under different conditions, the timing of their activation, and the possible identity of the elusive trigger that controls mitotic entry in human cells.

scholarly journals A novel form of Deleted in breast cancer 1 (DBC1) lacking the N-terminal domain does not bind SIRT1 and is dynamically regulated in vivo

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Leonardo Santos ◽  
Laura Colman ◽  
Paola Contreras ◽  
Claudia C. Chini ◽  
Adriana Carlomagno ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cell Cycle ◽  
Liver Regeneration ◽  
Partial Hepatectomy ◽  
Normal Cell ◽  
Cell Cycle Progression ◽  
Cycle Progression ◽  
Quiescent Cells ◽  
Normal Cell Cycle

Abstract The protein Deleted in Breast Cancer-1 is a regulator of several transcription factors and epigenetic regulators, including HDAC3, Rev-erb-alpha, PARP1 and SIRT1. It is well known that DBC1 regulates its targets, including SIRT1, by protein-protein interaction. However, little is known about how DBC1 biological activity is regulated. In this work, we show that in quiescent cells DBC1 is proteolytically cleaved, producing a protein (DN-DBC1) that misses the S1-like domain and no longer binds to SIRT1. DN-DBC1 is also found in vivo in mouse and human tissues. Interestingly, DN-DBC1 is cleared once quiescent cells re-enter to the cell cycle. Using a model of liver regeneration after partial hepatectomy, we found that DN-DBC1 is down-regulated in vivo during regeneration. In fact, WT mice show a decrease in SIRT1 activity during liver regeneration, coincidentally with DN-DBC1 downregulation and the appearance of full length DBC1. This effect on SIRT1 activity was not observed in DBC1 KO mice. Finally, we found that DBC1 KO mice have altered cell cycle progression and liver regeneration after partial hepatectomy, suggesting that DBC1/DN-DBC1 transitions play a role in normal cell cycle progression in vivo after cells leave quiescence. We propose that quiescent cells express DN-DBC1, which either replaces or coexist with the full-length protein, and that restoring of DBC1 is required for normal cell cycle progression in vitro and in vivo. Our results describe for the first time in vivo a naturally occurring form of DBC1, which does not bind SIRT1 and is dynamically regulated, thus contributing to redefine the knowledge about its function.

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