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Since complex formation between c-Src and CSK seemed a likely regulatory step in the control of c-Src kinase activity, such an association was investigated by immunoprecipitation and Western blotting as well as intracellular localization studies. Although some portions of CSK were found in a membrane fraction, no complex formation between CSK and c-Src was observed, suggesting that the src homology 2 domain of CSK does not play a role in the direct interaction of c-Src.</jats:p>","journal":"Proceedings of the National Academy of Sciences","year":1992,"id":594969,"datarank":0.6907755278982138,"base_score":4.605170185988092,"endowment":4.605170185988092,"self_citation_contribution":0.6907755278982138,"citation_network_contribution":0.0,"self_endowment_contribution":0.6907755278982138,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":99,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1523320,"name":"B Knudsen","orcid":null,"position":1,"is_corresponding":false},{"id":1523321,"name":"M Okada","orcid":null,"position":2,"is_corresponding":false},{"id":1523322,"name":"S Nada","orcid":null,"position":3,"is_corresponding":false},{"id":1523324,"name":"H Nakagawa","orcid":null,"position":4,"is_corresponding":false},{"id":1523325,"name":"H Hanafusa","orcid":null,"position":5,"is_corresponding":false},{"id":1523319,"name":"H Sabe","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Molecular cloning and expression of chicken C-terminal Src kinase: lack of stable association with c-Src protein.","abstract":"<jats:p>Cloning and sequencing of chicken C-terminal Src kinase (CSK), a tyrosine kinase that phosphorylates the regulatory C-terminal tyrosine residue present on cytoplasmic tyrosine kinases of the Src family, demonstrated a high degree of interspecies conservation as well as src homology 2 and 3 domains N-terminal to the kinase domain. The lack of autophosphorylation sites distinguishes CSK from other tyrosine kinases. CSK is unique and does not belong to a gene family, suggesting that it may phosphorylate other members of the Src family of tyrosine kinases in addition to c-Src. Since complex formation between c-Src and CSK seemed a likely regulatory step in the control of c-Src kinase activity, such an association was investigated by immunoprecipitation and Western blotting as well as intracellular localization studies. 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