Maintenance of the Golgi apparatus (GA) structure and function depends on Golgi matrix proteins. The posttranslational modification of Golgi proteins such as phosphorylation of members of the golgin and GRASP families is important for determining Golgi architecture. Some Golgi proteins including golgin-84 are also known to be methylated, but the function of golgin methylation remains unclear. Here, we show that the protein arginine methyltransferase 5 (PRMT5) localizes to the GA and forms complexes with several components involved in GA ribbon formation and vesicle tethering. PRMT5 interacts with the golgin GM130, and depletion of PRMT5 causes defects in Golgi ribbon formation. Furthermore, PRMT5 methylates N-terminal arginines in GM130, and such arginine methylation appears critical for GA ribbon formation. Our findings reveal a molecular mechanism by which PRMT5-dependent arginine methylation of GM130 controls the maintenance of GA architecture.
Graphene, with its properties of intrinsic flexibility, reliable electrical performance, and high chemical stability, is highly desirable as bioelectrodes for detecting electrophysiological signals. However, its mechanical properties limit its application to a great extentenergy dissipation mechanisms are not provided by the carbon network for external strain and it easily cracks. Herein, inspired by the very structure of the avian nest, we report a durable and nondisposable transparent graphene skin electrode for detecting electrophysiological signals, which was fabricated by semi-embedding highly graphitized electrospun fiber/monolayer graphene (GFG) into soft elastomer. Because of the semi-embedded structure and strong interaction between annealed electrospun fiber and graphene through graphitization, as-fabricated conductive film demonstrated high conductivity and transparency (∼150 Ω/□ at 83% transmittance), as well as a stable electrical performance under mechanical vibrations (strain, peel-off, stir, etc.). It can be used to reliably collect vital biometric signals, such as electrocardiogram (ECG), surface electromyogram (sEMG), and electroencephalogram (EEG). Furthermore, the semi-embedded GFG in the elastomer demonstrated excellent washability (rinsing/stirring in water) and repeatability (∼10 repeats) with high signal-to-noise ratio (up to 30 dB) while detecting sEMG. This is the first report of durable and transparent graphene skin electrode for biometric signals detection, revealing potential opportunities in wearable healthcare applications.
The Slit-Robo GTPase-activating proteins (srGAPs) are critical for neuronal migration through inactivation of Rho GTPases Cdc42, Rac1, and RhoA. Here we report that srGAP2 physically interacts with protein arginine methyltransferase 5 (PRMT5). srGAP2 localizes to the cytoplasm and plasma membrane protrusion. srGAP2 knockdown reduces cell adhesion spreading and increases cell migration, but has no effect on cell proliferation. PRMT5 binds to the N terminus of srGAP2 (225-538 aa) and methylates its C-terminal arginine residue Arg-927. The methylation mutant srGAP2-R927A fails to rescue the cell spreading rate, is unable to localize to the plasma membrane leading edge, and perturbs srGAP2 homodimer formation mediated by the F-BAR domain. These results suggest that srGAP2 arginine methylation plays important roles in cell spreading and cell migration through influencing membrane protrusion.Cell migration is essential for a wide variety of physiological and pathological processes such as embryonic development, wound tissue repair, and tumor metastasis (1-2). Classically, the major driving force for migration in mammalian cells is thought to be provided by actin polymerization at the cell protrusion of the front edge and F-actin depolymerization to retract cell body at the rear (3). These coordinated processes are regulated by small Rho GTPases, especially Cdc42, Rac1, and RhoA (4 -5). Similar to other GTPases, Rho GTPases act as intracellular molecular switches, cycling between a GDPbound inactive form and a GTP-bound active form. The two interconvertible forms are controlled by two classes of proteins, guanine nucleotide exchange factors (GEFs), 2 which promote the exchange of GDP for GTP, and GTPase-activating proteins (GAPs), which increase the GTPase activity of Rho GTPases through converting GTP to GDP, thereby closing the switch (6 -7).srGAP is a family of RhoGAP proteins, identified in the SlitRobo signal pathway. The srGAP family consists of three members, srGAP1, -2, and -3. All of them possess three conserved domains, F-BAR, RhoGAP, and SH3 (8). The function of RhoGAP domain of srGAP family protein is extensively studied because of its role in the negative regulation of Rho GTPase activities important for cytoskeleton rearrangement (8 -9). In addition to the RhoGAP domain, studies have found that the F-BAR domain-containing proteins function as key regulators in membrane remodeling in eukaryotes. Each of these proteins shares a similar quaternary "banana-like" structure, which forms elongated dimers mediated by the anti-parallel association of ␣ helices in each monomer (10 -11). Moreover, positive charges within the "banana-like" structure are aligned to interact with negative charges of the membrane via electrostatic interactions (12). Therefore, the F-BAR domains act as membrane-associated scaffolds and deform cell membrane independently of its F-actin bundling activity (13-14).Based on structural characteristics and phylogenetic analysis, the BAR domain super family includes "classical" BAR domain, F-BAR...
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