Publications by authors named "Han Nim Lee"

The ubiquitin-binding NBR1 autophagy receptor plays a prominent role in recognizing ubiquitylated protein aggregates for vacuolar degradation by macroautophagy. Here, we show that upon exposing plants to intense light, NBR1 associates with photodamaged chloroplasts independently of ATG7, a core component of the canonical autophagy machinery. NBR1 coats both the surface and interior of chloroplasts, which is then followed by direct engulfment of the organelles into the central vacuole via a microautophagy-type process.

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Phosphatidylinositol 3-phosphate (PI3P) is a signaling phospholipid that play a key role in endomembrane trafficking, specifically autophagy and endosomal trafficking. However, the mechanisms underlying the contribution of PI3P downstream effectors to plant autophagy remain unknown. Known PI3P effectors for autophagy in include ATG18A (Autophagy-related 18A) and FYVE2 (Fab1p, YOTB, Vac1p, and EEA1 2), which are implicated in autophagosome biogenesis.

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Autophagy is an intracellular trafficking mechanism by which cytosolic macromolecules and organelles are sequestered into autophagosomes for degradation inside the vacuole. In various eukaryotes including yeast, metazoans, and plants, the precursor of the autophagosome, termed the phagophore, nucleates in the vicinity of the endoplasmic reticulum (ER) with the participation of phosphatidylinositol 3-phosphate (PI3P) and the coat protein complex II (COPII). Here we show that Arabidopsis thaliana FYVE2, a plant-specific PI3P-binding protein, provides a functional link between the COPII machinery and autophagy.

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Pollen wall assembly is crucial for pollen development and plant fertility. The durable biopolymer sporopollenin and the constituents of the tryphine coat are delivered to developing pollen grains by the highly coordinated secretory activity of the surrounding tapetal cells. The role of membrane trafficking in this process, however, is largely unknown.

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Fluorescence properties of a molecule can be used to study the structural and functional nature of biological processes. Physical properties, including fluorescence lifetime, emission spectrum, emission polarization, and others, help researchers probe a molecule, produce desired effects, and infer causes and consequences. Correlative imaging techniques such as hyperdimensional imaging microscopy (HDIM) combine the physical properties and biochemical states of a fluorophore.

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Phosphatidylinositol-3-phosphate (PI3P) is a signaling phospholipid enriched in the membranes of late endosomes (LE) and vacuoles. PI3P mediates vacuolar and endosomal trafficking through recruiting PI3P-binding effector proteins to the LE. PI3P is produced from phosphatidylinositol by the PI 3-kinase complex containing VACUOLAR PROTEIN SORTING 34 (VPS34).

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Article Synopsis
  • Aggrephagy is a selective autophagy process that helps manage protein aggregates during cell stress, crucial for protein quality control.
  • The study investigates the role of the NBR1 protein in Arabidopsis, finding it is not essential for all types of autophagy but is necessary for forming autophagic vesicles under heat stress.
  • NBR1 is proposed to act as a receptor for aggrephagy in plants, helping to maintain protein balance during both stress and normal conditions.
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BPH1 acts as a substrate receptor of CRL3 complex and negatively regulates ABA-mediated cellular responses. The study on its function provides information that helps further understand the relationship between ABA signaling and UPS. Abscisic acid (ABA) plays a crucial role in a variety of cellular processes, including seed dormancy, inhibition of seedling growth, and drought resistance in plants.

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Phosphatidylinositol 3-P (PI3P) is a signaling molecule that controls a variety of processes in endosomal, autophagic, and vacuolar/lysosomal trafficking in yeasts and mammals. Vacuolar protein sorting 34 (Vps34) is a conserved PI3K present in multiple complexes with specific functions and regulation. In yeast, the PI3K complex II consists of Vps34p, Vps15p, Vps30p/Atg6p, and Vps38p, and is essential for vacuolar protein sorting.

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Autophagy targets cytoplasmic cargo to a lytic compartment for degradation. Autophagy-related (Atg) proteins, including the transmembrane protein Atg9, are involved in different steps of autophagy in yeast and mammalian cells. Functional classification of core Atg proteins in plants has not been clearly confirmed, partly because of the limited availability of reliable assays for monitoring autophagic flux.

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Article Synopsis
  • * The transition between peroxisome types involves breaking down old enzymes through proteolytic actions in different cellular areas.
  • * Recent studies in Arabidopsis seedlings suggest that peroxisomes can be selectively degraded through a process called pexophagy in the vacuole.
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Article Synopsis
  • Plant seedlings need to develop photosynthetic machinery before they can be classified as photoautotrophs.
  • Upon exposure to light, some plant cells undergo remodeling, during which certain peroxisomal proteins are degraded.
  • Recent research indicates that ATG7-dependent autophagy plays a partial role in the degradation of these outdated peroxisomal proteins as Arabidopsis seedlings grow.
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Article Synopsis
  • Plant peroxisomes are essential for seedling growth, breaking down fatty acids to supply carbon before photosynthesis begins.
  • As seedlings transition from using stored nutrients to photosynthesis, the enzyme makeup of peroxisomes changes, but the process for removing outdated proteins is not well understood.
  • This study provides evidence that autophagy, a process for degrading cellular components, plays a crucial role in managing peroxisome numbers in Arabidopsis thaliana hypocotyls during early growth.
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