Transcription Factor Deformed Wings Is an Atg8a-Interacting Protein That Regulates Autophagy.

LC3 (microtubule-associated protein 1 light chain 3, called Atg8 in yeast and ) is one of the most well-studied autophagy-related proteins. LC3 controls the selectivity of autophagic degradation by interacting with LIR (LC3-interacting region) motifs also known as AIM (Atg8-interacting motifs) on selective autophagy receptors that carry cargo for degradation. Although the function of Atg8 family proteins is primarily cytoplasmic, they are also enriched in the nucleus.

Atg8 family proteins, LIR/AIM motifs and other interaction modes.

The Atg8 family of ubiquitin-like proteins play pivotal roles in autophagy and other processes involving vesicle fusion and transport where the lysosome/vacuole is the end station. Nuclear roles of Atg8 proteins are also emerging. Here, we review the structural and functional features of Atg8 family proteins and their protein-protein interaction modes in model organisms such as yeast, and to humans.

Antibacterial activity of vB_AbaM_PhT2 phage hydrophobic amino acid fusion endolysin, combined with colistin against Acinetobacter baumannii.

Phage lytic enzymes are promising antimicrobial agents. In this study, an endolysin derived from vB_AbaM_PhT2 (vPhT2), was identified. This endolysin represented the conserved lysozyme domain.

A yeast two-hybrid screening identifies novel Atg8a interactors in .

Macroautophagy/autophagy-related protein Atg8/LC3 is important for autophagosome biogenesis and required for selective degradation of various substrates. In our recent study, we performed a yeast two-hybrid screening to identify proteins that interact with Atg8a, the homolog of Atg8/LC3. The screening identified several Atg8a-interacting proteins.

Selective autophagy controls innate immune response through a TAK1/TAB2/SH3PX1 axis.

Selective autophagy is a catabolic route that turns over specific cellular material for degradation by lysosomes, and whose role in the regulation of innate immunity is largely unexplored. Here, we show that the apical kinase of the Drosophila immune deficiency (IMD) pathway Tak1, as well as its co-activator Tab2, are both selective autophagy substrates that interact with the autophagy protein Atg8a. We also present a role for the Atg8a-interacting protein Sh3px1 in the downregulation of the IMD pathway, by facilitating targeting of the Tak1/Tab2 complex to the autophagy platform through its interaction with Tab2.

Assays to Monitor Mitophagy in Drosophila.

Autophagy is a central pathway utilized by many eukaryotic cells in order to recycle intracellular constituents, particularly under periods of nutrient scarcity or cellular damage. The process is evolutionarily conserved from yeast to mammals and can be highly selective with regard to the contents that are targeted for degradation. The availability of Drosophila transgenic lines and fluorophore-labeled autophagic markers allows nowadays for the more effortless visualization of the process within cells.

Caspase involvement in autophagy.

Caspases are a family of cysteine proteases widely known as the principal mediators of the apoptotic cell death response, but considerably less so as the contributors to the regulation of pathways outside cellular demise. In regards to autophagy, the modulatory roles of caspases have only recently begun to be adequately described. In contrast to apoptosis, autophagy promotes cell survival by providing energy and nutrients through the lysosomal degradation of cytoplasmic constituents.

Immuno-Gold Labeling of Drosophila Follicles for Transmission Electron Microscopy.

Detecting the localization of cellular components using gold nanoparticles has come to offer tremendous advantages in cell biology, allowing for the high resolution imaging of the cellular organization at the subcellular level. This is further aided by the breakthroughs in the cryopreparation of samples, which focus at the retention of antigenicity in efforts to mirror the native state of the tissues and cells as closely as possible. Herein, we describe the methodology for immuno-gold labeling of Drosophila follicles, following preparation of the samples using the Tokuyasu method for ultracryosectioning.