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Chang, J.-Y.

Publications and source records attributed to Chang, J.-Y..

4 recordsLinked to original sources

Kinetic Control of Nuclear-encoded Mitochondrial mRNA Localization and Local Translation

Most biological processes are dynamic, yet experimental methods predominantly rely on steady-state measurements to investigate their underlying mechanisms. RNA localization is a fundamental aspect of eukaryotic cell organization and is dynamically regulated by cells. While extensively studied in specialized cell types for a limited number of candidate RNAs, the general principles governing dynamic RNA localization at a transcriptome-wide scale remain largely unexplored. Existing transcriptome-wide studies provide only a static snapshot of RNAs residing in specific cellular locales, in part due to the limited availability of tools for probing cellular spatial organization at biologically relevant scales. Here, we leverage the high spatial (tens of nanometers) and temporal (minute) resolution of APEX-seq to quantitatively measure the dependence of RNA transport on molecular motors at a transcriptome-wide scale in living cells. We conducted these experiments in the context of the localization of mRNAs to the mitochondria, which are essential for cellular function. Our findings indicate that the majority of nuclear-encoded RNAs encoding mitochondrial proteins localize to the outer mitochondrial membrane (OMM) for local translation. We reveal a crucial role of retrograde dynein-based motor transport in RNA localization, demonstrating that its disruption severely impairs RNA targeting to the OMM. Time-resolved profiling of RNAs at the OMM revealed that localization is an active process, and even a brief disruption of transport for a few minutes results in a dramatic loss of localization. Moreover, we demonstrate that the translation efficiency (TE) of localized RNAs is a critical determinant of RNA localization in the context of motor-driven transport, as RNAs that delocalize following motor-transport perturbations exhibit lower TE. Using our temporal perturbation data, we also developed a spatiotemporal model that utilizes translation kinetics to capture key features of RNA localization dynamics at the OMM. Together, experiments and modeling suggest that the process of local translation at the OMM is kinetically controlled by the cell, and reveal an unappreciated mechanism by which active transport of RNAs enables cells to modulate their translation within minutes through RNA localization control. Our study demonstrates how simultaneously capturing the kinetics of hundreds of transcripts with minute resolution can uncover general principles of cellular and organelle organization. Together, these experiments and modeling reveal how active transport and translation jointly maintain the OMM-localized transcriptome. More broadly, they identify RNA localization to cellular membranes as a rapidly tunable mechanism for controlling local translation, even in non-polarized cells.

cell biology↗

Characterization of Clinical Fusobacterium nucleatum Isolates from Oral Squamous Cell Carcinoma Patients

Fusobacterium nucleatum (Fn), a Gram-negative anaerobe primarily residing in the oral cavity, has garnered increasing attention for its role in a broad spectrum of human diseases. While typically absent or rarely detected outside the oral cavity in healthy individuals, Fn is frequently found at extra-oral sites under disease conditions and has been implicated in cancer progression and prognosis1. In oral squamous cell carcinoma (OSCC), the abundance of Fn significantly increases as the disease progresses, promoting cell invasion and metastasis. Furthermore, substantial evidence links Fn to accelerated tumor growth and metastatic progression in colorectal cancer (CRC), where its presence is also associated with chemotherapy resistance and poor prognosis. Here, to further elucidate the pathogenic mechanisms of Fn in cancer progression, this study characterized the physiological traits, virulence factor expression, and impacts on cancer cells of 10 Fn strains, including two well-characterized ATCC strains and eight clinical isolates. The clinical isolates consisted of three strains from saliva samples of 117 OSCC patients and five strains from 160 non-cancer individuals. Results indicated that oral isolates, regardless of disease origin, all belong to Fn subspecies polymorphum. The ATCC strains (23726 and 25586) exhibited shorter cell lengths and faster growth rates compared to the clinical isolates. Both ATCC strains formed stable biofilms and expressed key virulence genes, including aim1, fadA, fomA, and radD. All isolates tested showed sensitivity to a panel of eight different antibiotics. Interestingly, only one clinical isolate displayed similar stimulation of CRC cell migration as the two ATCC strains, while the other seven displayed no such ability. Collectively, these findings suggest that the most virulent strains, in terms of biofilm formation and virulence gene expression, are not necessarily the most pathogenic in the context of cancer cell interactions. Future pan-genomic analyses, incorporating whole-genome sequencing of the clinical isolates, will aim to delineate the genetic determinants contributing to the carcinogenic potential of Fn.

microbiology↗

The protease interpain A of Prevotella intermedia promotes human OSCC cells proliferation and migration

Prevotella intermedia has been increasingly recognized as a potential contributor to oral squamous cell carcinoma (OSCC), yet the underlying mechanisms remain poorly defined. In this study, we identified interpain A (InpA), a cysteine protease secreted by P. intermedia, as a key virulence factor that promotes oral epithelial cell proliferation and OSCC cell migration. Conditioned medium (CM) derived from P. intermedia strain ATCC 25611 enhanced proliferation in both normal oral keratinocytes (SG cells) and OSCC cell lines (SCC-15, SAS). The pro-proliferative effect was abolished upon heat inactivation of the CM and inhibited by E64, a cysteine protease inhibitor, and FSLLRY-NH2, a PAR-2 antagonist, suggesting the involvement of protease-activated receptor-2 (PAR-2) signaling. InpA was highly secreted by strain ATCC 25611 but not by clinical isolates lacking proliferative effects, and RT-qPCR confirmed higher inpA expression in OSCC-derived strains compared to non-cancer controls. Recombinant InpA (rInpA) mimicked the effect of CM, inducing proliferation and migration, which were blocked by PAR-2 inhibition. Transcriptomic and protein-level screening in SG cells revealed activation of EGFR and downstream RAS-RAF-MEK-ERK signaling. Furthermore, in a colorectal cancer (CRC) mouse model, oral administration of P. intermedia led to increased tumor formation, suggesting a broader oncogenic potential. These findings highlight InpA as a PAR-2-activating protease that may contribute to OSCC and potentially other cancers associated with oral microbiota dysbiosis.

cancer biology↗

An atypical F-actin capping protein modulates cytoskeleton behaviors crucial to colonization of Trichomonas vaginalis

Cytoadherence and consequential migration are crucial for pathogens to establish colonization in the host. In contrast to the nonadherent isolate of Trichomonas vaginalis, the adherent one expresses more actin-related machinery proteins with more active flagellate-amoeboid morphogenesis, amoeba migration, and cytoadherence, activities that were abrogated by an actin assembly blocker. By immunoprecipitation coupled with label-free quantitative proteomics, an F-actin capping protein (TvFACP) was identified from the actin-centric interactome, with an atypically greater binding preference to G-actin than F-actin. TvFACP partially colocalized with F-actin at the parasite pseudopodia protrusion and formed the protein complexes with -actin through its c-terminal domain. Meanwhile, TvFACP overexpression suppresses F-actin polymerization, amoeboid morphogenesis, and cytoadherence in this parasite. Ser2 phosphorylation of TvFACP enriched in the amoeboid stage of adhered trophozoites was reduced by a CKII inhibitor. The site-directed mutagenesis and CKII inhibitor treatment revealed that Ser2 phosphorylation acts as a switching signal to alter TvFACP actin-binding activity and consequent actin cytoskeleton behaviors. Through CKII signaling, TvFACP also controls the conversion of adherent trophozoite from amoeboid migration to flagellate form with axonemal motility. Together, CKII-dependent Ser2 phosphorylation regulates TvFACP binding actin to fine-tune cytoskeleton dynamics and drive crucial behaviors underlying host colonization of T. vaginalis.

microbiology↗