The Scribble polarity protein stabilizes E-cadherin/p120-catenin binding and blocks retrieval of E-cadherin to the Golgi.

Lohia M, Qin Y, Macara IG
PLoS One. 2012 7 (11): e51130

PMID: 23226478 · PMCID: PMC3511384 · DOI:10.1371/journal.pone.0051130

Several polarity proteins, including Scribble (Scrb) have been implicated in control of vesicle traffic, and in particular the endocytosis of E-cadherin, but through unknown mechanisms. We now show that depletion of Scrb enhances endocytosis of E-cadherin by weakening the E-cadherin-p120catenin interaction. Unexpectedly, however, the internalized E-cadherin is not degraded but accumulates in the Golgi apparatus. Silencing p120-catenin causes degradation of E-cadherin in lysosomes, but degradation is blocked by the co-depletion of Scrb, which diverts the internalized E-cadherin to the Golgi. Loss of Scrb also enhances E-cadherin binding to retromer components, and retromer is required for Golgi accumulation of Scrb, and E-cadherin stability. These data identify a novel and unanticipated function for Scrb in blocking retromer-mediated diversion of E-cadherin to the Golgi. They provide evidence that polarity proteins can modify the intracellular itinerary for endocytosed membrane proteins.

MeSH Terms (16)

Animals Cadherins Catenins Cell Nucleus Cell Polarity Endocytosis Golgi Apparatus Humans Lysosomes Madin Darby Canine Kidney Cells Membrane Proteins Models, Biological Protein Binding Protein Stability Protein Transport Vesicular Transport Proteins

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