Ubiquitin and the Biology of the Cell
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Loss of cell polarity is one of the most fundamental mechanisms of cancer metastasis. Although polarized cells differ substantially in their morphology and function, it is an evolutionary conserved interaction network of polarity proteins that mediates polarity. We study what regulates the interactions, localization and activity of polarity proteins. This may enable us to manipulate polarity protein function with small organic compounds and offer new options for cancer therapy.
This structural information forms the basis for in vitro and in vivo experiments to address functional aspects.
Structural biology of ubiquitin-dependent protein degradation. Stacks were acquired every 5 s over 2 min and mitochondria movement tracked over at least five frames.
Ubiquitin - Wikipedia
Densitometry was performed using Quantity One V4. E on February 20, ER-associated protein degradation. Flag-tagged Gp Flag-Gp78 containing a CS mutation in the Ring finger domain. This article is distributed by The American Society for Cell Biology under license from the author s. Two months after publication it is available to the public under an Attribution—Noncommercial—Share Alike 3.
Structural biology of ubiquitin-dependent protein degradation
Molecular Biology of the Cell Vol. This is the final version - click for previous version. Min Fu Search for more papers by this author. Pascal St-Pierre Search for more papers by this author.
Jay Shankar Search for more papers by this author. Peter T. Wang Search for more papers by this author. Bharat Joshi Search for more papers by this author. Ivan R. Nabi Search for more papers by this author.
Add to favorites Download Citations Track Citations. Abstract Glycoprotein 78 Gp78 is a critical E3 ubiquitin ligase in endoplasmic reticulum—associated degradation. Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum.
J Cell Biol , Localization of autocrine motility factor receptor to caveolae and clathrin-independent internalization of its ligand to smooth endoplasmic reticulum. Mol Biol Cell 9 , Autocrine motility factor receptor is a marker for a distinct tubular membrane organelle.
OPA1 requires mitofusin 1 to promote mitochondrial fusion. Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin.
Nature , Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission. J Biol Chem , Studies on the mechanism of autophagy: formation of the autophagic vacuole. Mol Biosyst 5 , The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum.
Role of the Ubiquitin-Proteasome Systems in the Biology and Virulence of Protozoan Parasites
RING finger ubiquitin protein ligases: implications for tumorigenesis, metastasis and for molecular targets in cancer. Semin Cancer Biol 13 , Cell Death Differ 18 , Hum Mol Genet 19 , Nat Cell Biol 12 , Reversible interactions between smooth domains of the endoplasmic reticulum and mitochondria are regulated by physiological cytosolic calcium levels.
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J Cell Sci , A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation. Nat Cell Biol 11 , A role for KAI1 in promotion of cell proliferation and mammary gland hyperplasia by the gp78 ubiquitin ligase. LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
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EMBO J 19 , Protein degradation plays a critical role in cell signaling. The stability of many regulatory proteins including transcriptional factors is under tight control for proper signal transduction. Selective degradation of proteins is carried out by the ubiquitin-proteasome pathway. Specificity of this pathway is largely determined by E3 ubiquitin ligases. They share similar structure features: N-terminal C2 domain, C-terminal catalytic HECT domain and WW domains in the middle to mediate protein-protein interaction with substrates.
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