Abstract：
:Notch signaling is a conserved signaling pathway implicated in embryogenesis and adult tissue maintenance. Notch signaling strength is strictly regulated, notably by maintaining a controlled pool of functional receptor at the cell surface. Mammalian non-activated Notch receptor is internalized, ubiquitylated by the Itch E3 ubiquitin ligase and degraded in the lysosomes. Here, we show that β-arrestins are necessary for Itch-Notch interaction and for Itch-driven ubiquitylation and degradation of Notch. Interestingly, β-arrestins do not directly bind Itch but heterodimerize with a member of another subfamily of arrestins called ARRDC1 or α-arrestin 1, which harbors PPxY motifs that allow direct interaction with Itch. Cells transfected with ARRDC1 mutated in PPxY motifs show reduced Itch-mediated Notch ubiquitylation and impaired lysosomal degradation of Notch, as observed in β-arrestin(-/-) or Itch(-/-) cells. Our data show for the first time that ARRDC1 and β-arrestins heterodimerize and cooperate in the same complex to promote non-activated Notch receptor degradation, thus acting as negative regulators of Notch signaling.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Puca L,Chastagner P,Meas-Yedid V,Israël A,Brou Cdoi
10.1242/jcs.130500subject
Has Abstractpub_date
2013-10-01 00:00:00pages
4457-68issue
Pt 19eissn
0021-9533issn
1477-9137pii
jcs.130500journal_volume
126pub_type
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