PMID: 2501314Jul 1, 1989Paper

Regulation of desmosome assembly in epithelial cells: kinetics of synthesis, transport, and stabilization of desmoglein I, a major protein of the membrane core domain

The Journal of Cell Biology
M Pasdar, W J Nelson

Abstract

Desmosomes are composed of two morphologically and biochemically distinct domains, a cytoplasmic plaque and membrane core. We have initiated a study of the synthesis and assembly of these domains in Madin-Darby canine kidney (MDCK) epithelial cells to understand the mechanisms involved in the formation of desmosomes. Previously, we reported the kinetics of assembly of two components of the cytoplasmic plaque domain, Desmoplakin I/II (Pasdar, M., and W. J. Nelson. 1988. J. Cell Biol. 106:677-685 and 106:687-699. We have now extended this analysis to include a major glycoprotein component of the membrane core domain, Desmoglein I (DGI; Mr = 150,000). Using metabolic labeling and inhibitors of glycoprotein processing and intracellular transport, we show that DGI biosynthesis is a sequential process with defined stages. In the absence of cell-cell contact, DGI enters a Triton X-100 soluble pool and is core glycosylated. The soluble DGI is then transported to the Golgi complex where it is first complex glycosylated and then titrated into an insoluble pool. The insoluble pool of DGI is subsequently transported to the plasma membrane and is degraded rapidly (t1/2 less than 4 h). Although this biosynthetic pathway occurs independently ...Continue Reading

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Citations

Feb 5, 1996·The Journal of Comparative Neurology·A Mackay-SimS C Kinnamon
Jan 1, 1992·Cell Motility and the Cytoskeleton·M PasdarK A Krzeminski
Oct 1, 1994·Journal of Surgical Oncology·S NatsugoeT Fukumoto
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