The Golgi apparatus is a membranous organelle in the cell that plays essential roles in protein and lipid trafficking, sorting, processing, and modification. Its basic structure is a stack of closely aligned flattened cisternae. In mammalian cells, dozens of Golgi stacks are often laterally linked into a ribbon-like structure. Biogenesis of the Golgi during cell division occurs through a sophisticated disassembly and reassembly process that can be divided into three distinct but cooperative steps, including the deformation and reformation of the Golgi cisternae, stacks, and ribbon. Here, we review our current understanding of the protein machineries that control these three steps in the cycle of mammalian cell division: GRASP65 and GRASP55 in Golgi stack and ribbon formation; ubiquitin and AAA ATPases in postmitotic Golgi membrane fusion; and golgins and cytoskeleton in Golgi ribbon formation.
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http://dx.doi.org/10.1016/j.tcb.2013.01.008 | DOI Listing |
J Med Virol
January 2025
Department of Microbiology, Howard University College of Medicine, Washington, District of Columbia, USA.
SARS-CoV-2 Envelope (E) protein is critical in viral assembly, release, and virulence. E gene was considered highly conserved and evolving slowly. Pan-sarbecoviruses-conserved regions in the E gene have been used as targets for various RT-PCR assays to detect SARS-CoV-2.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
Key Laboratory of Horticultural Crop Germplasm Innovation and Utilization (Co-Construction by Ministry and Province), Key Laboratory of Horticultural Crop Genetic Improvement and Eco-physiology of Anhui Province, Institute of Horticulture, Anhui Academy of Agricultural Sciences, Hefei 230031, China. Electronic address:
Seed hardness is an important quality characteristic of pomegranate fruit. The development of seed hardness relies on the deposition of lignin in the inner seed coat, but the underlying molecular mechanisms remain unclear. In this study, we identified a member of ABCG transporters, PgABCG9, which may function in seed hardening by negatively regulating lignin biosynthesis.
View Article and Find Full Text PDFACS Omega
December 2024
Laboratorio de Glicobiología y Diagnóstico Molecular, Centro de Investigación en Dinámica Celular, Universidad Autónoma del Estado de Morelos, Av. Universidad 1001, Col. Chamilpa, Cuernavaca 62209, Morelos, México.
The human CMP-sialic acid transporter (hCST) is a mammalian highly conserved type III antiporter that translocates CMP-sialic acid into the Golgi lumen, supporting sialylation. Although different works have focused on elucidating structure-function relationships in the hCST, this is the first study to address them in an alternatively spliced isoform. We have previously reported the expression of a functional human del177 isoform that has skipping of exon 6, resulting in a loss of 59 amino acids, without change in the open reading frame and conserving its C-terminal region.
View Article and Find Full Text PDFFront Cell Dev Biol
December 2024
Departments of Biology, University of York, York, United Kingdom.
-glycosylation plays a crucial role in defining the pharmacological properties and efficacy of therapeutic proteins, commonly referred to as biologics. The inherent complexity and lack of a templated process in glycosylation leads to a wide variation in glycan structures, posing significant challenges in achieving consistent glycan profiles on biologics. This study leverages omics technologies to predict which cell lines are likely to yield optimal glycosylation profiles, based on the existing knowledge of the functional impact of specific glycan structures on the pharmacokinetics, immunogenicity, and stability of therapeutic antibodies.
View Article and Find Full Text PDFSci Rep
December 2024
Institute of Physiological Chemistry and Pathobiochemistry, University of Münster, Waldeyerstrasse 15, D-48149, Münster, Germany.
The heparan sulfate (HS)-rich extracellular matrix (ECM) serves as an initial interaction site for the homotrimeric spike (S) protein of SARS-CoV-2 to facilitate subsequent docking to angiotensin-converting enzyme 2 (ACE2) receptors and cellular infection. More recent variants, notably Omicron, have evolved by swapping several amino acids to positively charged residues to enhance the interaction of the S-protein trimer with the negatively charged HS. However, these enhanced interactions may reduce Omicron's ability to move through the HS-rich ECM to effectively find ACE2 receptors and infect cells, raising the question of how to mechanistically explain HS-associated viral movement.
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