ARL4D Peptide
- Known as:
- ARL4D Peptide
- Catalog number:
- 42-757P
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- ARL4D Peptide
Related genes to: ARL4D Peptide
- Gene:
- ARL4D NIH gene
- Name:
- ADP ribosylation factor like GTPase 4D
- Previous symbol:
- ARF4L
- Synonyms:
- -
- Chromosome:
- 17q21.31
- Locus Type:
- gene with protein product
- Date approved:
- 1995-08-23
- Date modifiied:
- 2015-11-19
Related products to: ARL4D Peptide
Related articles to: ARL4D Peptide
- The rising incidence of CINIII, particularly in younger patients, has highlighted limitations of current surgical treatments, which can affect fertility and carry recurrence risks. This underscores an urgent clinical need for non-invasive therapies. Our study addresses this by investigating the cellular and molecular changes during CINIII progression to cervical squamous cell carcinoma (CSCC). We employed single-cell sequencing to meticulously analyze cell types and molecular mechanisms within cervical epithelial cells and their microenvironment throughout the CINIII-to-CSCC transition. Key findings include the identification of Sox2 and its signaling pathway as markers for specific cervical stem cells (CCSCs) during malignant transformation. In the microenvironment, upregulated VWF, MMP2, and HTRA1 were observed in vascular endothelial cells, while TXNIP+ and ARL4D+ fibroblasts underwent transformation into myofibroblasts. Immune cell proportions notably increased, particularly macrophages, T cells, B cells, NK cells, mast cells, and neutrophils, contrasting with a decrease in non-immune cells. Furthermore, interaction analysis revealed that communication between macrophages and cervical epithelial cells was the most prominent. This research comprehensively details the complex cellular and molecular remodeling inherent in CINIII progression. By pinpointing specific pathways and cell populations, our findings establish a crucial framework for developing innovative, non-invasive drug therapies to delay disease progression and ultimately improve long-term reproductive outcomes for patients. - Source: PubMed
Publication date: 2026/05/21
Ma YaomeiZhang SuLiu BeiLiu YiboHe YuchaoGong WenchenChen WenshuaiQi LishaWang KeGuo Hua - The high mortality rate of metastatic cutaneous melanoma (SKCM) remains a major challenge in clinical treatment. This study used single-cell RNA sequencing (scRNA-Seq) technology to compare the differences between metastatic and primary tumour cells. By manually annotating cell types, significant disparities in cell communication patterns and functional pathways between the two groups were identified. Combined with transcriptomic data, differential gene analysis was performed to screen out a core gene set associated with tumour metastasis. To achieve accurate prediction of tumour metastasis, this study innovatively constructed a binary classification algorithm (PSO-SVM) integrating particle swarm optimisation (PSO) and support vector machines (SVMs). This model optimises SVM parameters via the PSO algorithm, addressing the limitations of traditional machine learning models such as insufficient accuracy and poor generalization ability in tumour metastasis prediction. Verified by comparison with mainstream machine learning methods, the PSO-SVM model exhibited superior classification performance and successfully identified five key metastasis-related genes: SFN, S100A8, KLF5, ARL4D and TINCR. Furthermore, the expression differences of these genes in the metastatic group were verified at the single-cell level, clarifying their regulatory roles in different cell types and states. Through an innovative analytical strategy integrating single-cell and transcriptomic data, this study elucidated the core molecular mechanisms of SKCM metastasis and key regulatory pathways in the tumour microenvironment, providing potential biomarkers and therapeutic targets for the early diagnosis and targeted treatment of SKCM metastasis. This PSO-SVM-integrated analysis method also offers new insights for research on metastasis mechanisms of other cancers. - Source: PubMed
Liao ZhiweiChen WeimingHe YingdiZheng YichenChen XiaonanShen Han - Self-association by small GTPases on membrane is critical for their signaling output and cellular function. However, a mechanistic understanding of how membrane components regulate this process remains incompletely understood. Here, we show that phosphatidylinositol 4,5-bisphosphate [PI(4,5)P] promotes Arl4D self-association to potentiate downstream Pak1 signaling. We first show that Arl4D self-association is GTP-dependent and occurs at the plasma membrane. Fibronectin stimulation increases this self-association through two cooperative mechanisms: i) direct binding of PI(4,5)P by Arl4D via a conserved C-terminal polybasic motif, and ii) phosphorylation of Arl4D at Ser144 by its effector kinase Pak1. As a result, Arl4D membrane residency and protein stability are enhanced, with downstream signaling through Pak1 also amplified. Furthermore, pursuing structural prediction using AlphaFold, we generate an Arl4D mutant defective in self-association but retains GTP binding and membrane targeting, and find that this mutant fails to activate Pak1 for cell migration, while forced self-association of this mutant restores these downstream effects. Collectively, our findings reveal how an extracellular matrix cue leads to directional cell migration through Arl4D assembling into signaling-competent multimers at the plasma membrane, with cooperation between lipid recognition and kinase-mediated feedback playing critical roles. - Source: PubMed
Publication date: 2026/03/04
Chang Ting-WeiLee Fang-Jen S - ADP-ribosylation factor-like 4D (Arl4D), a Ras small GTPases superfamily member, plays crucial roles in membrane trafficking, cytoskeletal remodeling and cell migration. GDP-bound Arl4D has previously been shown to locate at the mitochondria and alter mitochondrial morphology and activity; however, how the nucleotide-binding state and mitochondrial targeting of Arl4D is regulated had remained unclear. We now discover that TBC1D15, a well-known Rab7 GTPase-activating protein (GAP), functions also as an Arl4D GAP to promote Arl4D mitochondrial targeting. We initially show that GDP-bound Arl4D translocates to the mitochondria under serum starvation and affects mitochondrial homeostasis. We also show that TBC1D15 interacts with Arl4D through the TBC domain and promotes GTP hydrolysis of Arl4D. Knockdown of TBC1D15 leads to an increase in Arl4D activity and decreased Arl4D mitochondrial translocation under serum starvation. These findings support the hypothesis that TBC1D15 acts as an Arl4D GAP and reveal a new role for this GAP in modulating mitochondrial homeostasis. - Source: PubMed
Publication date: 2026/03/12
Chen Chia-TangLiu Tsai-JungLin Shin-JinChang Ting-WeiLee Fang-Jen S - Activation of extracellular signal-regulated kinases 1 and 2 (Erk1/2; also known as MAPK3 and MAPK1, respectively) at the plasma membrane usually leads to their translocation to various intracellular sites, where scaffolding proteins mediate substrate targeting. However, in platelet-derived growth factor (PDGF)-induced signaling, Erk1/2 phosphorylate Pak1 to drive cell migration while remaining at the plasma membrane, raising the question of whether scaffolding proteins are required. Similarly, the small GTPase Arf-like protein 4D (Arl4D) promotes cell migration by recruiting Pak1 to the plasma membrane and facilitating its phosphorylation, although the mechanism linking recruitment to phosphorylation remains unclear. To address these questions, we show that Arl4D functions as a scaffolding protein by recruiting Erk1/2 and Pak1 to the plasma membrane, assembling them into a functional complex. This complex allows Erk1/2 to phosphorylate Pak1, supporting the role of the latter in cell migration. Our findings identify Arl4D as a novel regulator of Erk1/2, reveal a conserved role of scaffolding proteins in Erk1/2 substrate targeting, and uncover an unrecognized interplay among Arl4D, Erk1/2 and Pak1. These insights provide a deeper understanding of the molecular coordination underlying Pak1-mediated cell migration and its regulation by Erk1/2 and Arl4D. - Source: PubMed
Publication date: 2025/05/22
Chang Ting-WeiLin Ming-ChiehYu Chia-JungLee Fang-Jen S