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    Keywords: CELL-MIGRATION ; ACTIN CYTOSKELETON ; EPIDERMAL-GROWTH-FACTOR ; PROTEOMIC ANALYSIS ; TUMOR-SUPPRESSOR ; ALPHA-5-BETA-1 INTEGRIN ; COATED PITS ; RECEPTOR-MEDIATED ENDOCYTOSIS ; MOTOR PROTEINS ; LYSOSOMAL DEGRADATION
    Abstract: alpha2beta1 integrin is one of the most important collagen-binding receptors, and it has been implicated in numerous thrombotic and immune diseases. alpha2beta1 integrin is a potent tumour suppressor, and its downregulation is associated with increased metastasis and poor prognosis in breast cancer. Currently, very little is known about the mechanism that regulates the cell-surface expression and trafficking of alpha2beta1 integrin. Here, using a quantitative fluorescence-microscopy-based RNAi assay, we investigated the impact of 386 cytoskeleton-associated or -regulatory genes on alpha2 integrin endocytosis and found that 122 of these affected the intracellular accumulation of alpha2 integrin. Of these, 83 were found to be putative regulators of alpha2 integrin trafficking and/or expression, with no observed effect on the internalization of epidermal growth factor (EGF) or transferrin. Further interrogation and validation of the siRNA screen revealed a role for KIF15, a microtubule-based molecular motor, as a significant inhibitor of the endocytic trafficking of alpha2 integrin. Our data suggest a novel role for KIF15 in mediating plasma membrane localization of the alternative clathrin adaptor Dab2, thus impinging on pathways that regulate alpha2 integrin internalization.
    Type of Publication: Journal article published
    PubMed ID: 24659801
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