Publications by authors named "Huilong Yin"

Background: Tumor-associated macrophages (TAMs) significantly influence the progression, metastasis, and recurrence of esophageal squamous cell carcinoma (ESCC). The aberrant expression of long noncoding RNAs (lncRNAs) in ESCC has been established, yet the role of lncRNAs in TAM reprogramming during ESCC progression remains largely unexplored.

Methods: ESCC TAM-related lncRNAs were identified by intersecting differentially expressed lncRNAs with immune-related lncRNAs and performing immune cell infiltration analysis.

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Article Synopsis
  • * Reducing METTL3 levels in macrophages protects mice from colitis by enhancing the expression of phosphoglycolate phosphatase (PGP), which reprograms glucose metabolism and reduces differentiation of harmful CD4+ T helper 1 (Th1) cells.
  • * Two new METTL3 inhibitors, F039-0002 and 7460-0250, show promise in alleviating colitis symptoms, indicating that targeting METTL3 could be a viable strategy for managing intestinal
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Alzheimer's disease (AD) is a heterogeneous disease with complex clinicopathological characteristics. To date, the role of m6A RNA methylation in monocyte-derived macrophages involved in the progression of AD is unknown. In our study, we found that methyltransferase-like 3 (METTL3) deficiency in monocyte-derived macrophages improved cognitive function in an amyloid beta (Aβ)-induced AD mouse model.

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Hepatic glycogen is the main source of blood glucose and controls the intervals between meals in mammals. Hepatic glycogen storage in mammalian pups is insufficient compared to their adult counterparts; however, the detailed molecular mechanism is poorly understood. Here, we show that, similar to glycogen storage pattern, N6-methyladenosine (m6A) modification in mRNAs gradually increases during the growth of mice in liver.

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N6-methyladenosine (m6A) is a reversible mRNA modification that has been shown to play important roles in various biological processes. However, the roles of m6A modification in macrophages are still unknown. Here, we discover that ablation of Mettl3 in myeloid cells promotes tumour growth and metastasis in vivo.

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Enhancer of Zeste Homolog 2 (EZH2), a key epigenetic regulator, is involved in breast cancer progression and metastasis. LOXL4 is increasingly recognized as an important player in cancer progression. To date, how EZH2 regulates LOXL4 in the progression of breast cancer remains unclear.

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We have recently reported that Rootletin prevents Cep68 from VHL-mediated proteasomal degradation to maintain centrosome cohesion, unveiling the first underlying mechanism of a linker protein required for maintenance of centrosome cohesion. The minichromosome maintenance (MCM) proteins 2-7 have long been noticed to localize to centrosomes, but their functions at the centrosome are presently unknown. Here, we show that MCM7 directly binds to the centrosomal linker protein Cep68 in vitro and complexes with Cep68 and VHL in vivo.

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Centrosome cohesion, mostly regarded as a proteinaceous linker between parental centrioles, ensures the interphase centrosome(s) to function as a single microtubule-organizing center. Maintenance of centrosome cohesion counts on a number of centrosomal linker proteins because depletion of any of those leads to premature centrosome separation in interphase, termed centrosome splitting. However, the underlying mechanisms of the dependence are unknown.

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We have previously reported that the centriolar protein centlein functions as a molecular link between C-Nap1 and Cep68 to maintain centrosome cohesion [1]. In this study, we identified centlein as a novel microtubule-associated protein (MAP), directly binding to purified microtubules (MTs) via its longest coiled-coil domain. Overexpression of centlein caused profound nocodazole- and cold-resistant MT bundles, which also relied on its MT-binding domain.

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Centrosome cohesion, mostly regarded as a proteinaceous linker between parental centrioles, ensures that the interphase centrosome(s) function as a single microtubule-organizing center. Impairment of centrosome cohesion leads to the splitting of centrosomes. Although the list of cohesion proteins is growing, the precise composition and regulation of centrosome cohesion are still largely unknown.

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