{"doi":"10.1128/mcb.16.7.3465","title":"Regulation of Btk by Src Family Tyrosine Kinases","abstract":null,"journal":"Molecular and Cellular Biology","year":1996,"id":602903,"datarank":0.6980940525236285,"base_score":4.653960350157523,"endowment":4.653960350157523,"self_citation_contribution":0.6980940525236285,"citation_network_contribution":0.0,"self_endowment_contribution":0.6980940525236285,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":104,"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":1084785,"name":"Hyunsun Park","orcid":"0000-0003-1338-654X","position":1,"is_corresponding":false},{"id":1546450,"name":"Brian W. Howell","orcid":null,"position":2,"is_corresponding":false},{"id":108918,"name":"David J. Rawlings","orcid":"0000-0002-0810-1776","position":3,"is_corresponding":false},{"id":1222428,"name":"Jonathan Cooper","orcid":null,"position":4,"is_corresponding":false},{"id":304228,"name":"Owen N. Witte","orcid":"0000-0003-4461-4533","position":5,"is_corresponding":false},{"id":1546449,"name":"Daniel E. H. Afar","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Regulation of Btk by Src Family Tyrosine Kinases","abstract":"Loss of function of Bruton's tyrosine kinase (Btk) results in X-linked immunodeficiencies characterized by a broad spectrum of signaling defects, including those dependent on Src family kinase-linked cell surface receptors. A gain-of-function mutant, Btk*, induces the growth of fibroblasts in soft agar and relieves the interleukin-5 dependence of a pre-B-cell line. To genetically define Btk signaling pathways, we used a strategy to either activate or inactivate Src family kinases in fibroblasts that express Btk*. The transformation potential of Btk* was dramatically increased by coexpression with a partly activated c-Src mutant (E-378 --> G). This synergy was further potentiated by deletion of the Btk Src homology 3 domain. Downregulation of Src family kinases by the C-terminal Src kinase (Csk) suppressed Btk* activation and biological potency. In contrast, kinase-inactive Csk (K-222 --> R), which functioned as a dominant negative molecule, synergized with Btk* in biological transformation. Activation of Btk* correlated with increased phosphotyrosine on transphosphorylation and autophosphorylation sites. These findings suggest that the Src and Btk kinase families form specific signaling units in tissues in which both are expressed.","is_dataset_classified":null,"base_score":4.653960350157523,"endowment":4.653960350157523,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"8668162","pmcid":"PMC231341","openalex_id":"https://openalex.org/W1807266461","authors":[],"funders":[{"funder_name":"PHS HHS","grant_id":"R019102","title":null},{"funder_name":"NCI NIH HHS","grant_id":"CA12800","title":null},{"funder_name":"NCI NIH HHS","grant_id":"CA41072","title":null}],"total_grants":3,"fwci":4.389,"citation_percentile":0.94958092,"influential_citations":0,"citation_trend":[{"year":2012,"count":5},{"year":2013,"count":6},{"year":2014,"count":2},{"year":2015,"count":2},{"year":2016,"count":5},{"year":2018,"count":1},{"year":2019,"count":2},{"year":2020,"count":1},{"year":2021,"count":1},{"year":2022,"count":2}],"oa_status":"green","license":"https://journals.asm.org/non-commercial-tdm-license","oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/231341","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/231341","host_type":"repository"},{"url":"https://journals.asm.org/doi/pdf/10.1128/MCB.16.7.3465","host_type":"publisher"},{"url":"https://www.tandfonline.com/doi/pdf/10.1128/MCB.16.7.3465","host_type":"publisher"},{"url":"https://doi.org/10.1128/mcb.16.7.3465","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/8668162","host_type":"repository"}],"fields_of_study":["Immunodeficiency and Autoimmune Disorders","Chronic Lymphocytic Leukemia Research","Platelet Disorders and Treatments","Agammaglobulinaemia Tyrosine Kinase","Animals","Blotting, Western","CSK Tyrosine-Protein Kinase","Cell Line","Humans","Peptide Mapping","Phosphopeptides","Phosphorylation","Point Mutation","Protein-Tyrosine Kinases","Proto-Oncogene Proteins pp60(c-src)","Rats","Recombinant Proteins","Transfection","src-Family Kinases"],"mesh_terms":["Agammaglobulinaemia Tyrosine Kinase","CSK Tyrosine-Protein Kinase","Animals","Cell Line","Humans","Peptide Mapping","Phosphopeptides","Phosphorylation","Protein-Tyrosine Kinases","Recombinant Proteins","Transfection","Blotting, Western","Proto-Oncogene Proteins pp60(c-src)","Point Mutation","src-Family Kinases","Rats"],"keywords":["Bruton's tyrosine kinase","Proto-oncogene tyrosine-protein kinase Src","Autophosphorylation","Tyrosine kinase","Src family kinase","Biology","Cell biology","Tyrosine-protein kinase CSK","Kinase","SH3 domain","Cancer research","Signal transduction","Protein kinase A"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"doi"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-29T20:35:36.939717Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}