GORASP1 293T Cell Transient Overexpression Lysate(Denatured)
- Known as:
- GORASP1 293T Cell Transient Overexpression Lysate(Denatured)
- Catalog number:
- H00064689-T01
- Product Quantity:
- 100 uL
- Category:
- -
- Supplier:
- Abno
- Gene target:
- GORASP1 293T Cell Transient Overexpression Lysate(Denatured)
Related genes to: GORASP1 293T Cell Transient Overexpression Lysate(Denatured)
- Gene:
- GORASP1 NIH gene
- Name:
- golgi reassembly stacking protein 1
- Previous symbol:
- GOLPH5
- Synonyms:
- GRASP65, P65, FLJ23443
- Chromosome:
- 3p22.2
- Locus Type:
- gene with protein product
- Date approved:
- 2001-11-02
- Date modifiied:
- 2016-10-05
Related products to: GORASP1 293T Cell Transient Overexpression Lysate(Denatured)
Related articles to: GORASP1 293T Cell Transient Overexpression Lysate(Denatured)
- We recently demonstrated that the endoplasmic reticulum export of proTGFα (encoded by TGFA) is tightly gated and that proteostasis factors, including the intramembrane protease RHBDL4 (also known as RHBDD1), can promote its release by an unknown mechanism. While investigating a potential link between RHBDL4-regulated p24 (TMED) family proteins and proTGFα trafficking, we uncovered an RHBDL4-independent pathway in which the cargo receptor TMED9 induces unconventional protein secretion (UcPS) of ectopically expressed proTGFα. This pathway selectively requires GRASP65 (also known as GORASP1), but not the closely related GRASP55 (or GORASP2), and depends on components of the autophagic machinery and the ESCRT-associated protein ALIX (also known as PDCD6IP), consistent with a Golgi-bypass secretion route. TMED9- and GRASP65-induced proTGFα secretion is insensitive to brefeldin A treatment and involves trafficking through pre-Golgi compartments. Although largely based on overexpression systems, our findings identify a previously unrecognized UcPS mechanism and provide insight into alternative protein trafficking pathways that might be exploited under conditions of proteostasis stress and in pathological contexts such as cancer and inflammation. At present, our data establish the existence of a TMED9- and GRASP65-dependent Golgi-bypass trafficking route under conditions of ectopic cargo expression, whereas its endogenous physiological relevance remains to be established. - Source: PubMed
Publication date: 2026/08/28
Steigleder Susanne SDöring IsabelTauber MarinaNüchel JulianLemberg Marius K - Golgi Reassembly and Stacking Proteins (GRASP) have been associated with Golgi-ribbon structure and unconventional vesicular protein secretion. In performing these functions, GRASPs consistently interact with membranes. The presence of lipid modifications, such as myristoylation, is a crucial consideration for obtaining detailed information about the interactions between GRASPs and membranes. Nonetheless, it has been overlooked in the literature so far. Here, we describe a reconstitution protocol for myristoylated human GRASP65 and GRASP55 in lipid model membranes, enabling investigation of their interactions using techniques ranging from structural characterization to spectroscopy and microscopy. Our results showed that myristoyl-anchored GRASPs can influence lipid packing, membrane dynamics, and hydration, suggesting a possible role for their disordered SPR domains in these interactions. - Source: PubMed
Publication date: 2026/05/05
Kava EmanuelMalacrida LeonelDíaz MarcelaItri RosangelaCosta-Filho Antonio J - Lysosomes are multifunctional organelles that play important roles in cellular recycling, signaling, and homeostasis, relying on precise trafficking and activation of lysosomal enzymes. While the Golgi apparatus plays a central role in lysosomal enzyme sorting, the mechanisms linking Golgi function to lysosomal activity remain incompletely understood. Here, we identify the Golgi-resident protein GRASP55, but not its paralog GRASP65, as necessary for lysosome function. Loss of GRASP55 expression leads to missorting and secretion of lysosomal enzymes, lysosomal dysfunction and bloating. GRASP55 deficiency also disrupts lysosomal mTORC1 signaling, reducing the phosphorylation of its lysosomal substrates TFEB/TFE3, while sparing its non-lysosomal targets. Mechanistically, GRASP55 binds and maintains the COPI adaptor GOLPH3 protein at the Golgi, thereby controlling the Golgi localization and stability of LYSET and GNPTAB that are required for mannose 6-phosphate (M6P) tagging of lysosomal enzymes. These findings reveal an essential role for GRASP55 in Golgi-lysosome communication and lysosomal enzyme trafficking and underscore the importance of Golgi-mediated protein sorting in lysosome function and lysosomal mTORC1 signaling. - Source: PubMed
Publication date: 2026/04/16
Nüchel JulianOmidi MaryamFernandes Stephanie ATauber MarinaPohl SandraPlomann MarkusDemetriades Constantinos - The Golgi complex is central to cellular homeostasis and serves as a key processing and sorting hub for protein trafficking. In many cell types, the Golgi complex is organized as interconnected stacks of cisternae, forming a structure known as the Golgi ribbon. This ribbon undergoes dynamic remodelling during physiological processes, such as cell division, and under pathological conditions, including cancer and neurodegeneration. A critical step in the unlinking of the Golgi ribbon involves the phosphorylation of the stacking protein GRASP65, which leads to the separation of the ribbon into individual stacks, a process necessary for the G2/M transition of the cell cycle. However, existing tools for selectively manipulating the GRASP65 role in ribbon organization are limited by non-specific effects or technical challenges. Here, we present the development and characterization of a membrane-permeable peptide, R-GRASP65-S277, derived from GRASP65 and containing the phosphorylation site Ser277, which is essential for Golgi unlinking. This peptide effectively inhibited Golgi unlinking and mitotic entry in several cell lines, including cancer models. In contrast, a control peptide with a non-phosphorylatable alanine substitution (R-GRASP65-S277A) showed no such effect, confirming the specificity of the tool. Furthermore, the R-GRASP65-S277 peptide reversed Golgi unlinking induced by the chemotherapeutic agent doxorubicin, demonstrating its utility in studying stress-induced Golgi disassembly. These findings establish the R8-GRASP65-S277 peptide as a specific, potent, and scalable tool for probing the molecular mechanisms of Golgi unlinking, its regulation of cell cycle progression, and its potential contributions to pathological states. - Source: PubMed
Publication date: 2025/12/01
Cervigni Romina InesBonavita RaffaellaBarretta Maria LuisaSpano DanielaAyala InmaculadaMascanzoni FabiolaIannitti RobertaHenklein PetraMonti AlessandraRenna MaurizioDoti NunziannaColanzi Antonino - Taurine is an amino acid with several physiological functions and has been shown to be involved in the anti-tumor of human nasopharyngeal carcinoma (NPC) cells. However, the role of taurine metabolism-related genes (TMRGs) in NPC has not been reported. We integrated data from the Genecards, Kyoto Encyclopedia of Genes and Genomes (KEGG), and Gene Expression Omnibus(GEO) databases to identify differentially expressed genes associated with taurine metabolism in NPC patients. Gene Ontology (GO) and KEGG analyses were conducted to investigate the underlying mechanisms. Subsequently, Cox regression and Least Absolute Shrinkage and Selection Operator (LASSO) regression analyses were performed to construct a taurine metabolism-related prognostic signature. Survival, medication sensitivity, and immunological microenvironment evaluations were performed to assess the prognostic utility of the model. Finally, immunohistochemistry (IHC) experiments were performed to validate the model's prognostic reliability. In addition, we further verified the reliability of our research results through molecular docking and single-cell sequencing. Our prognostic model was based on three pivotal TMRGs (ABCB1, GORASP1, and EZH2). Functional analysis revealed a strong association between TMRGs and miRNAs in cancer. Notably, increased risk scores correlated with worsening tumor malignancy and prognosis. Significant disparities in immune microenvironment, immune checkpoints, and drug sensitivity were observed between the high- and low-risk groups. The protein expression patterns of the selected genes in clinical NPC samples were validated using immunohistochemistry. Molecular docking verified the interaction between these three core genes and taurine, which was further supported by single-cell sequencing showing significant expression variation among different cell clusters in NPC. We had elucidated the functions, therapeutic potential, and prognostic significance of three key genes related to taurine metabolism in NPC through multidimensional research and experimental validation. This research provided valuable insights and potential avenues for improved NPC management. - Source: PubMed
Publication date: 2025/04/24
Feng ZhangYang YuhangLuo WenqiLi JinqingXie ZhenlianZuo LongDuan MeijiaoZuo DongzhiMo RuweiTang XuejingYi ShijiangHe XiaosongLiu FangxianMa NingHe Feng