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Signal transduction and exercise
Published in Adam P. Sharples, James P. Morton, Henning Wackerhage, Molecular Exercise Physiology, 2022
Brendan Egan, Adam P. Sharples
When inactive, the initiation factors eIF3 and eIF4 are bound to the signalling proteins S6K1 and 4E-BP1, respectively. Resistance exercise, in particular, nutrients such as essential amino acids, and hormones such as insulin, all activate mTORC1, which, in turn, phosphorylates S6K1 and 4E-BP1 (and various other proteins in the mTOR signalling pathway). As a consequence, eIF3 and eIF4 detach from S6K1 and 4E-BP1 and contribute to the assembly of ribosomes.
EIF3D promoted cervical carcinoma through Warburg effect by interacting with GRP78
Published in Journal of Obstetrics and Gynaecology, 2023
Qing Liu, Jing Liu, Dan Zheng, Ranxi Zhang, Yan Xiang, Fei Xu, Xiaochan Zhou, Juan Qin
To date, the eukaryotic translation initiation factor 3 subunit D (EIF3D) is the non-core subunit of EIF3 that has received the least attention (Huang et al.2019). It involves many processes such as translation initiation and termination, as well as ribosome recovery (Lamper et al.2020). Zhang et al. showed that EIF3D promoted disease progression of gallbladder cancer (Zhang et al.2017). Gao et al. suggested that EIF3D plays an oncogenic role in development and progression of prostate cancer (Gao et al.2015). EIF3D has been found to be associated with the tumorigenesis and development, and widely expressed in a variety of tumour tissue cells, regulating the tumour cell cycle, and dysregulating the apoptotic and anti-apoptotic signalling pathways by increasing apoptosis (Lee et al.2016). So, this study investigated the possible effects of EIF3D on cell progression of cervical carcinoma and its underlying mechanism in vivo and vitro models.
RNA N6-methyladenosine methylation and skin diseases
Published in Autoimmunity, 2023
Yaqin Yu, Shuang Lu, Hui Jin, Huan Zhu, Xingyu Wei, Tian Zhou, Ming Zhao
In addition to acting as a Writer, METTL3 promotes epidermal growth factor (EGFR) and the Hippo pathway effector TAZ translation by recruiting eukaryotic initiation factor 3 (eIF3) to the transcription initiation complex in human lung cancer cells [40]. In contrast to the RNA degradation-promotive function of YTHDF2, YTHDF1 recruits ribosomes to accelerate RNA translation and protein production [42,58]. Activities of YTHDF1 and YTHDF3 have been reported to synergistically improve translation efficiency [44]. YTHDC2 specifically recognises and binds to the GGACU motif of the target RNA, which improves translation efficiency and reduces its RNA abundance [47]. Fragile X mental retardation protein (FMR1), a sequence-context-dependent reader, binds to ribosomes and inhibits mRNA translation [53,54]. hnRNPC specifically binds to the 29 nt sequence in the 3’UTR region of amyloid beta precursor protein (APP) mRNA, thereby stabilising APP mRNA and facilitating its translation [49]. Multiple intracellular stresses can increase m6A modification of the 5’UTR, the binding of which to eIF3 can induce translation of intracellular mRNA in a cap-independent manner [55].
A novel compound heterozygous mutation of MYSM1 gene in a patient with bone marrow failure syndrome 4
Published in British Journal of Biomedical Science, 2021
X Zhan, A Zhao, B Wu, Y Yang, L Wan, P Tan, J Huang, Y Lu
MYSM1 includes 3 domains: SANT, SWIRM and JAB. The SANT domain is present in nuclear receptor co-repressors and in the subunits of many chromatin-remodelling complexes [18]. It has a strong structural similarity to the DNA-binding domain of Myb-related proteins [19]. Despite the overall similarity there are differences that indicate that the SANT domain is functionally divergent from the canonical Myb DNA-binding domain [20]. SWIRM domain is a small alpha-helical domain of about 85 amino acid residues containing a helix-turn helix motif and binds to DNA [21]. Members of JAB family are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This family is also known as the MPN domain [22] and PAD-1-like domain [23] JABP1 domain [24] or JAMM domain [25]. These are metalloenzymes that function as the ubiquitin isopeptidase/deubiquitinase in the ubiquitin-based signalling and protein turnover pathways in eukaryotes [25].