Role of insulin-like growth factor-1 (IGF-1) in regulating cell cycle progression

2009 ◽  
Vol 389 (1) ◽  
pp. 150-155 ◽  
Author(s):  
Qi-lin Ma ◽  
Tian-lun Yang ◽  
Ji-ye Yin ◽  
Zhen-yu Peng ◽  
Min Yu ◽  
...  
Cells ◽  
2021 ◽  
Vol 10 (12) ◽  
pp. 3327
Author(s):  
Zhixiang Wang

The cell cycle is the series of events that take place in a cell, which drives it to divide and produce two new daughter cells. The typical cell cycle in eukaryotes is composed of the following phases: G1, S, G2, and M phase. Cell cycle progression is mediated by cyclin-dependent kinases (Cdks) and their regulatory cyclin subunits. However, the driving force of cell cycle progression is growth factor-initiated signaling pathways that control the activity of various Cdk–cyclin complexes. While the mechanism underlying the role of growth factor signaling in G1 phase of cell cycle progression has been largely revealed due to early extensive research, little is known regarding the function and mechanism of growth factor signaling in regulating other phases of the cell cycle, including S, G2, and M phase. In this review, we briefly discuss the process of cell cycle progression through various phases, and we focus on the role of signaling pathways activated by growth factors and their receptor (mostly receptor tyrosine kinases) in regulating cell cycle progression through various phases.


2000 ◽  
Vol 36 (1) ◽  
pp. 101-111 ◽  
Author(s):  
Michael Karas ◽  
Hadar Amir ◽  
Daniel Fishman ◽  
Michael Danilenko ◽  
Shraga Segal ◽  
...  

1997 ◽  
Vol 17 (9) ◽  
pp. 5485-5498 ◽  
Author(s):  
M A Guthridge ◽  
P Bellosta ◽  
N Tavoloni ◽  
C Basilico

We have identified a novel type 2C serine-threonine phosphatase, FIN13, whose expression is induced by fibroblast growth factor 4 and serum in late G1 phase. The protein encoded by FIN13 cDNA includes N- and C-terminal domains with significant homologies to type 2C phosphatases, a domain homologous to collagen, and an acidic domain. FIN13 expression predominates in proliferating tissues. Bacterially expressed FIN13 and FIN13 expressed in mammalian cells exhibit serine-threonine phosphatase activity, which requires Mn2+ and is insensitive to inhibition by okadaic acid. FIN13 is localized in the nuclei of transiently transfected cells. Cotransfection of FIN13-expressing plasmids with a plasmid that expresses the neomycin resistance gene inhibits the growth of drug-resistant colonies in NIH 3T3, HeLa and Rat-1 cells. In transiently transfected cells, FIN13 inhibits DNA synthesis and results in the accumulation of cells in G1 and early S phases. Similarly, the induction of expression of FIN13 under the control of a tetracycline-regulated promoter in NIH 3T3 cells leads to growth inhibition, with accumulation of cells in G1 and early S phases. Thus, overexpression and/or unregulated expression of FIN13 inhibits cell cycle progression, indicating that the physiological role of this phosphatase may be that of regulating the orderly progression of cells through the mitotic cycle by dephosphorylating specific substrates which are important for cell proliferation.


2017 ◽  
Vol 232 (10) ◽  
pp. 2722-2730 ◽  
Author(s):  
Yingbo Lin ◽  
Hongyu Liu ◽  
Ahmed Waraky ◽  
Felix Haglund ◽  
Prasoon Agarwal ◽  
...  

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