LIFR acetylation and phosphorylation modify different functions in the maintenance of embryonic stem cell omnipotence.

On January 25th, cell Reports, an international academic journal, published online a research paper by Jing Naijun Research Group of the Institute of Biochemistry and Cell Biology of the Shanghai Institute of Life Sciences of the Chinese Academy of Sciences in collaboration with the Qin Qi Research Group of the Institute of Health Sciences, "Opposing roles of the institute of acetylation and phosphorylation in LIFR-dependent self-renewal growth signaling in mouse embryonic stem cells".
The paper reveals the presence of translated acetylation and phosphorylation modification of LIFR protein, which is essential for transmitting LIF signals and activating downstream Stat3 signals, while phosphorylation modification inhibits LIFR self-activation.
the work revealed how protein translation modification specifically functions in the maintenance of embryonic stem cell omnipotence in mice.
LIF signal is a critical signal for the omnipotence maintenance and self-renewal of embryonic stem cells in mice.
LIF transmits the LIF signal downstream and activates Stat3 by combining its subject LIFR and forming a gp130 bind.
, how LIFR responds to and transmits LIF/Stat3 signals is not yet clear.
Yunbo, an assistant researcher in the Jingyi group, and Wang Xiongjun, a postdoctoral fellow of Qin's research group, and Xiao Mingzhe, a doctoral student, carried out in-depth cooperation, and mass spectrometry identification found that the LIFR protein had acetylation and phosphorylation modification, which relied on LIF signal stimulation.
the study found that acetylation modification of LIFR is essential for transmitting LIF signals and activating downstream Stat3 signals.
When researchers simulated continuous acetylation of LIFR with a mutant, the mutant spontaneously activated the downstream Stat3 signal and maintained the all-powerful type of embryonic stem cells in mice, while the acetylized inactivated mutant blocked the transmission of the LIF/Stat3 signal path.
further studies have found phosphorylation modifications at the C-end of the LIFR, which inhibits the LIFR from recruiting JAK and activates the Stat3 signal, which is activated by the ERK signal.
when cells are treated with ERK inhibitors (one of the classic 2i), LIFR undergoes a dephosphorylation process that activates the LIFR and the downstream Stat3 signal path.
, liFR spontaneously activates the LIFR/Stat3 signal after mutation of the phosphate bit at the C-end.
shows that phosphorylation at the C-end of LIFR plays a role in inhibiting the spontaneous activation of LIFR.
this work explains some of the mechanisms by which 2i maintains the omnipotence of mouse embryonic stem cells, i.e. ERK inhibitors perform the functions maintained by activating the classic LIFR/Stat3 (not dependent on LIF stimulation) signaling path path.
this work has deepened the understanding of the omnipotence maintenance mechanism of embryonic stem cells in mice.
: LIFR translates and retouched to regulate the LIF/Stat3 signal path.
In the absence of LIF, there is phosphorylation modification at the C-end of LIFR, which spontaneously inhibits the activation of LIFR/Stat3, making the mESC more prone to differentiation;
in the presence of LIF, LIF stimulates the acetylation of LIFR to occur, thus activating the Stat3 signal that does not depend on THE phosphorylation modification, thus keeping mouse ES cells omnipotent.
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