2017
DOI: 10.1083/jcb.201712033
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When E-cadherin is away, centrosomes can play

Abstract: Vargas-Hurtado and Basto highlight recent work from Rhys et al. revealing how E-cadherin affects clustering of extra centrosomes.

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Cited by 3 publications
(4 citation statements)
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References 10 publications
(36 reference statements)
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“…It consists of the large extracellular and intracellular cytoplasmic structural domains and is highly expressed in epithelial cells. E‐cadherin is also an important component of the adhesion and tight junctions of epithelial cells 28–30 . Vargas‐Hurtado et al found that DDR1 promotes E‐cadherin stability by inhibiting integrin‐β1‐Src activation‐mediated E‐cadherin endocytosis.…”
Section: Resultsmentioning
confidence: 99%
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“…It consists of the large extracellular and intracellular cytoplasmic structural domains and is highly expressed in epithelial cells. E‐cadherin is also an important component of the adhesion and tight junctions of epithelial cells 28–30 . Vargas‐Hurtado et al found that DDR1 promotes E‐cadherin stability by inhibiting integrin‐β1‐Src activation‐mediated E‐cadherin endocytosis.…”
Section: Resultsmentioning
confidence: 99%
“…With small interfering RNA technology, that study also revealed that reduced DDR1 decreases E‐cadherin expression at adhesions and enhances E‐cadherin endocytosis. Along with increased Src tyrosine 418 phosphorylation at tight junctions, inhibition of Src activity can restore the endocytosis of E‐cadherin and stability of E‐cadherin at tight junctions 28 . In addition, DDR1 expression has been reported to increase the cortical actin structure and promote the adhesion structure stability, while DDR1 downregulation increases stress fibre apparatus, resulting in a decreased adhesion junction stability.…”
Section: Resultsmentioning
confidence: 99%
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