Phagolysosome biogenesis is driven by a series of interactions between phagosomes and organelles of the biosynthetic and endocytic pathways. The presence of endocytic markers on phagosomes suggests that phagosomes and endosomes share common structural and functional characteristics. In that line of thought, protein phosphorylation has been shown to be involved in regulatory aspects of the fusion properties of endosomes and other vacuolar organelles. To study further the mechanisms involved in phagolysosome biogenesis, we have investigated the presence of phagosome proteins that can be phosphorylated in vitro by endogenous phagosome-associated kinases. The results obtained show that proteins phosphorylated on tyrosine residues are present on phagosomes. Moreover, complex phosphorylation/dephosphorylation cycles appear to occur during phagolysosome biogenesis. The addition of endosome fractions to phagosomes inhibit the phosphorylation of phagosome proteins. These results suggest that phosphorylation and dephosphorylation events could play roles in the biogenesis of phagolysosomes and regulate, in part, the complex in vivo interactions between phagosomes and endosomes.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/s0014-5793(96)01213-6 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
ATG9 promotes autophagosome formation through interaction with LC3.
Biochem Biophys Res Commun
February 2025
Department of Immunology, School of Basic Medical Sciences, Anhui Medical University, Hefei, Anhui, China. Electronic address:
The autophagosome is a double-membrane organelle that executes macroautophagy. Previous studies have shown that the autophagosome formation is driven by autophagy-related genes, among which ATG9 is the only conserved transmembrane protein and has been shown to play a critical role in the autophagosome formation. However, how ATG9 binds to the growing autophagosome membrane has remained uncertain.
View Article and Find Full Text PDFComparative genomics analyses of Actinobacteriota identify Golgi phosphoprotein 3 (GPP34) as a widespread ancient protein family associated with sponge symbiosis.
Microbiome
January 2025
Department of Marine Biology, Leon H. Charney School of Marine Sciences, University of Haifa, Haifa, Israel.
Background: Sponges harbor microbial communities that play crucial roles in host health and ecology. However, the genetic adaptations that enable these symbiotic microorganisms to thrive within the sponge environment are still being elucidated. To understand these genetic adaptations, we conducted a comparative genomics analysis on 350 genomes of Actinobacteriota, a phylum commonly associated with sponges.
View Article and Find Full Text PDFAdvances in Aggrephagy: Mechanisms, Disease Implications, and Therapeutic Strategies.
J Cell Physiol
January 2025
Guangzhou Municipal and Guangdong Provincial Key Laboratory of Protein Modification and Degradation, School of Basic Medical Sciences, Guangzhou Medical University, Guangzhou, China.
The accumulation of misfolded proteins within cells leads to the formation of protein aggregates that disrupt normal cellular functions and contribute to a range of human pathologies, notably neurodegenerative disorders. Consequently, the investigation into the mechanisms of aggregate formation and their subsequent clearance is of considerable importance for the development of therapeutic strategies. The clearance of protein aggregates is predominantly achieved via the autophagy-lysosomal pathway, a process known as aggrephagy.
View Article and Find Full Text PDFATG9A facilitates the closure of mammalian autophagosomes.
J Cell Biol
February 2025
Autophagy, Inflammation and Metabolism Center of Biomedical Research Excellence, University of New Mexico Health Sciences Center, Albuquerque, NM, USA.
Canonical autophagy captures within specialized double-membrane organelles, termed autophagosomes, an array of cytoplasmic components destined for lysosomal degradation. An autophagosome is completed when the growing phagophore undergoes ESCRT-dependent membrane closure, a prerequisite for its subsequent fusion with endolysosomal organelles and degradation of the sequestered cargo. ATG9A, a key integral membrane protein of the autophagy pathway, is best known for its role in the formation and expansion of phagophores.
View Article and Find Full Text PDFNon-lytic spread of poliovirus requires the nonstructural protein 3CD.
mBio
January 2025
Department of Microbiology and Immunology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.
Unlabelled: Non-enveloped viruses like poliovirus (PV) have evolved the capacity to spread by non-lytic mechanisms. For PV, this mechanism exploits the host secretory autophagy pathway. Virions are selectively incorporated into autophagosomes, double-membrane vesicles that travel to the plasma membrane, fuse, and release single-membrane vesicles containing virions.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!