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• W2003451876 abstract "ABSTRACT The secreted molecule unc-6/netrin is important for guiding axon projections and cell migrations. unc-5 and unc-40/DCC are identified as receptors for unc-6/netrin . The downstream factors of unc-6 receptors are beginning to be elucidated, and some key factors have been identified in various organisms. Here, we showed that SRC-1 interacts with the cytosolic domain of UNC-5 through its SH2 domain. This interaction also requires the intact kinase activity of SRC-1. Downregulation of src-1 by RNA interference decreases the biological processes initiated by the UNC-5 protein and decreases UNC-5 tyrosine phosphorylation. We also generated a chimeric protein consisting of the extracellular domain and transmembrane domain of UNC-5 and an intracellular domain of SRC-1. This fusion protein is able to partially rescue mutant phenotypes caused by unc-5 but not unc-6 , unc-40 , and unc-34 . Our results support a model in which SRC-1 is required for UNC-5-induced axon repulsion and gonad migration signaling pathways and in which localizing SRC-1 activity to UNC-5 is crucial for proper signal transduction in response to unc-6/netrin ." @default.
• W2003451876 created "2016-06-24" @default.
• W2003451876 creator A5016834516 @default.
• W2003451876 creator A5022490398 @default.
• W2003451876 creator A5039980094 @default.
• W2003451876 date "2005-08-01" @default.
• W2003451876 modified "2023-10-17" @default.
• W2003451876 title "SRC-1 Mediates UNC-5 Signaling in <i>Caenorhabditis elegans</i>" @default.
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• W2003451876 doi "https://doi.org/10.1128/mcb.25.15.6485-6495.2005" @default.
• W2003451876 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1190325" @default.
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