Sorting nexin 17 prevents lysosomal degradation of β1 integrins by binding to the β 1-integrin tail

Ralph Thomas Böttcher, Christopher Stremmel, Alexander Meves, Hannelore Meyer, Moritz Widmaier, Hui Yuan Tseng, Reinhard Fässler

Research output: Contribution to journalArticlepeer-review

129 Scopus citations


Integrin functions are controlled by regulating their affinity for ligand, and by the efficient recycling of intact integrins through endosomes. Here we demonstrate that the Kindlin-binding site in the β 1-integrin cytoplasmic domain serves as a molecular switch enabling the sequential binding of two FERM-domain-containing proteins in different cellular compartments. When β 1 integrins are at the plasma membrane, Kindlins control ligand-binding affinity. However, when they are internalized, Kindlins dissociate from integrins and sorting nexin 17 (SNX17) is recruited to free β 1-integrin tails in early endosomes to prevent β 1-integrin degradation, leading to their recycling back to the cell surface. Our results identify SNX17 as a β 1-integrin-tail- binding protein that interacts with the free Kindlin-binding site in endosomes to stabilize β 1 integrins, resulting in their recycling to the cell surface where they can be reused.

Original languageEnglish (US)
Pages (from-to)584-592
Number of pages9
JournalNature Cell Biology
Issue number6
StatePublished - Jun 2012

ASJC Scopus subject areas

  • Cell Biology


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