Keratins Turn over by Ubiquitination in a Phosphorylation-Modulated Fashion
نویسندگان
چکیده
منابع مشابه
Keratins Turn over by Ubiquitination in a Phosphorylation-Modulated Fashion
Keratin polypeptides 8 and 18 (K8/18) are intermediate filament (IF) proteins that are expressed in glandular epithelia. Although the mechanism of keratin turnover is poorly understood, caspase-mediated degradation of type I keratins occurs during apoptosis and the proteasome pathway has been indirectly implicated in keratin turnover based on colocalization of keratin-ubiquitin antibody stainin...
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Protein ubiquitination has been implicated in ATPdependent protein turnover and in a number of biological processes in eukaryotic cells. The ubiquitination activating enzyme, E l , and ubiquitin carrier protein, E2, are two essential enzymes in the protein ubiquitination machinery. Using purified E l and E2 from rabbit reticulocytes and various protein kinases, which include CAMP-dependent prot...
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BACKGROUND Transcription factor Oct1 regulates multiple cellular processes. It is known to be phosphorylated during the cell cycle and by stress, however the upstream kinases and downstream consequences are not well understood. One of these modified forms, phosphorylated at S335, lacks the ability to bind DNA. Other modification states besides phosphorylation have not been described. METHODOL...
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Maintenance of epithelial cell adhesion is crucial for epidermal morphogenesis and homeostasis and relies predominantly on the interaction of keratins with desmosomes. Although the importance of desmosomes to epidermal coherence and keratin organization is well established, the significance of keratins in desmosome organization has not been fully resolved. Here, we report that keratinocytes lac...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 2000
ISSN: 0021-9525,1540-8140
DOI: 10.1083/jcb.149.3.547