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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
While the functional relevance of these novel kinases and substrates in the work of Hoffman et al. (2015) (106) and Potts et al. (2017) (107) remains to be established, especially in the context of having a permissive role in the adaptive response to exercise, these findings highlight the possibility that much remains to be discovered about exercise-induced signal transduction in skeletal muscle. To this end, omics approaches allow the unbiased, large-scale identification of proteins that change their concentration or become modified in response to exercise. This allows researchers to develop new hypotheses and gain new insights into ways that are much faster than with one-target-at-a-time approaches. One recent example is an extension of the work of Potts et al. (2017) (107) by the same research group that resulted in the novel identification of TRIM28 and its Ser473 phosphorylation site as being activated by exercise and being a potential regulator of muscle size and function (albeit in non-physiological expression models in rodents) (108). Another notable finding was that the majority of contraction-induced phosphorylation events were rapamycin-insensitive (108), which is interpreted as further evidence for the emerging concept described above of mTORC-independent (i.e not dependant on mTORC) signal transduction pathways also being important for the regulation of skeletal muscle hypertrophy after loading (42).
Epigenetics from Oocytes to Embryos
Published in Carlos Simón, Carmen Rubio, Handbook of Genetic Diagnostic Technologies in Reproductive Medicine, 2022
Dagnė Daškevičiūtė, Marta Sanchez-Delgado, David Monk
Even though nuclear exclusion of DNMT1 is essential for passive demethylation in cleavage-stage embryos, genetic evidence implies it is still required for maintenance of ICR methylation, suggesting that it is not exclusively retained in the cytoplasm. The limited amounts of DNMT1, as well as DNMT3A/B, are targeted to ICR via the TRIM28/KAP1 co-repressive complex that exhibits sequence-specificity due to the zinc-finger proteins (ZFPs) ZFP57 and ZNF44531–34 (Figure 9.2c). Classically, ZFP-KAP1 complexes include the TRIM28/KAP1 scaffold protein, the histone methyltransferase SETDB1, the nucleosome remodeling histone deacetylation complex (NuRD), heterochromatin protein 1 (HP1), and the DNA methylation machinery, all of which are responsible for silencing of transposable elements, with underlying sequence-specificity attributed to unique combinations of ZFPs that target different retrotransposon families.35 Once recruited to a sequence, transcriptional repression is mediated by H3K9me3 and DNA methylation.36 ZFPs have been shown not only to recognize transposable elements, but an increasing number of these proteins also bind to single-copy regions in the genome as highlighted by ZFP57 and ZNF445.33,34
High Expression of TRIM15 Is Associated with Tumor Invasion and Predicts Poor Prognosis in Patients with Gastric Cancer
Published in Journal of Investigative Surgery, 2021
Weiran Zhou, Hao Chen, Yuanyuan Ruan, Xiaoqing Zeng, Fenglin Liu
Tripartite motif (TRIM) family proteins belong to a large conserved family and there are over 70 members. Several reviews described that TRIM proteins are implicated in plenty of cellular activities such as transcription, autophagy, carcinogenesis and so on [4–7]. The tripartite motif structure is consisted of a RING-finger domain, one or two B-box finger domains and a coiled-coil domain [8]. Because of the RING-finger domain, most of the TRIM proteins are characterized as E3 ubiquitin ligases [9]. Much of the research in the last decade has revealed that quite a lot of TRIM proteins are related to the malignancy of cancers including TRIM24, TRIM28 and TRIM29 [10–12]. It has been found that the expression of TRIM proteins was altered in prostate cancer, breast cancer and lung cancer [13–15].
SUMO: a novel target for anti-coronavirus therapy
Published in Pathogens and Global Health, 2021
The sumoylation of TRIM28 typically suppresses the transcription of endogenous retroviral (ERV) genes. IAV infection induces the loss of SUMO-modified TRIM28, a transcriptional repressor, thus promoting the expression of endogenous retroviral (ERV) RNAs that are sensed as non-self by host pattern recognition receptors (PRRs) [76,77] (Figure 4). Consequently, the derepression of ERVs transcription induces the subsequent activation of IFN-mediated antiviral response via the RIG-I-, MAVS-, TBK1-, and JAK1-dependent pathway [76]. TRIM28 may play a critical role in SARS-CoV-2’s entry into human cells [78]. It was recently reported that angiotensin-converting enzyme 2 (ACE2), which is co-expressed with TRIM28 in type II pneumocytes, is the cellular receptor protein for SARS-CoV-2 [79,80]. Also, the knockdown of TRIM28 stimulates ACE2 expression via IFN-γ dependent immune response [78]. Although the SUMO modification of TRIM28 has not been studied in coronavirus-infected cells, studying SUMO function in coronaviruses may provide clues to developing new therapies and life-saving vaccines for coronavirus diseases.