ArticleMolecular and cellular biology2012
β1 integrin NPXY motifs regulate kidney collecting-duct development and maintenance by induced-fit interactions with cytosolic proteins.
Article in Molecular and cellular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 11 citations in OpenAlex.
- Kindlins regulate integrin- and growth factor-dependent ureteric bud formation.Development (Cambridge, England) · 2026Article
- Ligand-independent integrin β1 signaling supports lung adenocarcinoma development.JCI insight · 2022Article
- The β8 integrin cytoplasmic domain activates extracellular matrix adhesion to promote brain neurovascular development.Development (Cambridge, England) · 2022Article
- A Novel Mutation in an NPXY Motif of β Integrin Reveals Phenotypes Similar toFrontiers in cell and developmental biology · 2019Article
- Talin regulates integrin β1-dependent and -independent cell functions in ureteric bud development.Development (Cambridge, England) · 2017Article
- Deletion of β1-integrin in collecting duct principal cells leads to tubular injury and renal medullary fibrosis.American journal of physiology. Renal physiology · 2017Article
- Article
- Integrin α3β1 regulates kidney collecting duct development via TRAF6-dependent K63-linked polyubiquitination of Akt.Molecular biology of the cell · 2015Article
- Epithelial β1 integrin is required for lung branching morphogenesis and alveolarization.Development (Cambridge, England) · 2014Article
- The integrin β1 subunit regulates paracellular permeability of kidney proximal tubule cells.The Journal of biological chemistry · 2014Article
- β1 integrins with individually disrupted cytoplasmic NPxY motifs are embryonic lethal but partially active in the epidermis.The Journal of investigative dermatology · 2013Article
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 3 countries.
Funding
Abstract
Loss of β1 integrin expression inhibits renal collecting-system development. Two highly conserved NPXY motifs in the distal β1 tail regulate integrin function by associating with phosphtyrosine binding (PTB) proteins, such as talin and kindlin. Here, we define the roles of these two tyrosines in collecting-system development and delineate the structural determinants of the distal β1 tail using nuclear magnetic resonance (NMR). Mice carrying alanine mutations have moderate renal collecting-system developmental abnormalities relative to β1-null mice. Phenylalanine mutations did not affect renal collecting-system development but increased susceptibility to renal injury. NMR spectra in bicelles showed the distal β1 tail is disordered and does not interact with the model membrane surface. Alanine or phenylalanine mutations did not alter β1 structure or interactions between α and β1 subunit transmembrane/cytoplasmic domains; however, they did decrease talin and kindlin binding. Thus, these studies highlight the fact that the functional roles of the NPXY motifs are organ dependent. Moreover, the β1 cytoplasmic tail, in the context of the adjacent transmembrane domain in bicelles, is significantly different from the more ordered, membrane-associated β3 integrin tail. Finally, tyrosine mutations of β1 NPXY motifs induce phenotypes by disrupting their interactions with critical integrin binding proteins like talins and kindlins.
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