Abstract

Cell migration is a fundamental property of great importance in many cell-biological events during embryogenesis as well as in wound healing and tumour metastasis. In all cell migration events, cells need to interact with the surrounding environment either through cell–cell interactions or cellular interactions with the extracellular matrix (ECM). A major group of receptors for the ECM are integrins, which are heterodimeric receptors comprising noncovalently associated α and β subunits. A number of integrins can share the same β subunit, whereas the α subunit confers integrin-specific properties to a particular α–β heterodimer. In integrin-mediated events, the cytoplasmic tails of the β subunits have been shown to be important in both cell signalling and cytoskeletal interactions. Integrin-specific effects also point to a role of the cytoplasmic tail of integrin α chains. In an elegant study by Alahari et al., evidence is presented for molecular interactions underlying the specific effects of α5β1.Using a yeast two-hybrid screen with the cytoplasmic tail of the integrin α5 chain as a bait, a novel protein, named Nischarin (from Sanskrit, connotes slowness of motion), that interacts with the integrin α5 chain was identified from an embryonic mouse expression library 1xNischarin, a novel protein that interacts with the integrin α5 subunit and inhibits cell migration. Alahari, S.K et al. J. Cell Biol. 2000; 151: 1141–1154Crossref | PubMed | Scopus (87)See all

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