ILK, PINCH and parvin: the tIPP of integrin signalling
By K. Legate, Eloi Montañez, O. Kudlacek, Reinhard Füssler. Nature reviews. Molecular cell biology, 2006
725 citations recorded by the source corpus.
Subfields: Cell Biology, Immunology and Allergy, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/6f010953385d639fe31e341221af6ac44dcc4c4d
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In Cell Biology
- M. Schwartz
- Matthias Mann
- M. Frame
- Gerhard Christofori
- V. Brunton
- K. Legate
- Mahmut Yilmaz
- R. Fässler
In Immunology and Allergy
In Molecular Biology
Citations in the corpus
- Integrins and extracellular matrix in mechanotransduction. (2010, background): “Kinase activities of integrin-linked kinase are uncertain as the kinase domain lacks catalytic residues that are normally conserved among protein kinases; however in vitro studies suggest there may be some catalytic activity, though this has not been identified in vivo.(41) Paxillin acts as an adapt”
- Genetic and cell biological analysis of integrin outside-in signaling. (2009, background): “Additional connections between ILK and the cytoskeleton can also form through paxillin, which in turn binds to parvin and vinculin (Legate et al. 2006).”
- E-cadherin–integrin crosstalk in cancer invasion and metastasis (2013, background): “This promotes dynamic actin and adhesion changes at the cell membrane, and activation of numerous downstream signalling pathways that have a pivotal function in cellular processes, such as adhesion, migration, proliferation and survival (Cabodi et al., 2010; Legate et al., 2006).”
- SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function. (2008, background): “A preformed complex consisting of the three proteins, ILK, PINCH, and Parvin, represents an important component of the integrin adhesion complex (Legate et al., 2006).”
- EMT, the cytoskeleton, and cancer cell invasion (2009, background): “Integrins are linked to the actin cytoskeleton and signal via the ternary complex of integrin-linked kinase (ILK), pinch and parvin, also named the tIPP complex [107] (Fig.”
- Integrin Structure and Function (2010, background): “Cdc42 activity has been shown to be regulated by Src activity and ligand binding to integrins can activate Cdc42 via the ILK–Pinch–parvin complex (Legate et al. 2006).”