{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Harr MW"],"funding":["NCI NIH HHS"],"pagination":["165-177"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10569261"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7(3)"],"pubmed_abstract":["There is increasing evidence that the T-cell protein, Lck, is involved in the pathogenesis of chronic lymphocytic leukemia (CLL) as well as other leukemias and lymphomas. We previously discovered that Lck binds to domain 5 of inositol 1,4,5-trisphosphate receptors (IP<sub>3</sub>R) to regulate Ca<sup>2+</sup> homeostasis. Using bioinformatics, we targeted a region within domain 5 of IP<sub>3</sub>R-1 predicted to facilitate protein-protein interactions (PPIs). We generated a synthetic 21 amino acid peptide, KKRMDLVLELKNNASKLLLAI, which constitutes a domain 5 sub-domain (D5SD) of IP<sub>3</sub>R-1 that specifically binds Lck via its SH2 domain. With the addition of an HIV-TAT sequence to enable cell permeability of D5SD peptide, we observed wide-spread, Ca<sup>2+</sup>-dependent, cell killi"],"journal":["Archives of microbiology & immunology"],"pubmed_title":["A Novel Peptide that Disrupts the Lck-IP<sub>3</sub>R Protein-Protein Interaction Induces Widespread Cell Death in Leukemia and Lymphoma."],"pmcid":["PMC10569261"],"funding_grant_id":["R01 CA042755","T32 CA059366"],"pubmed_authors":["Harr MW","Haberer B","Zhong F","Aldabbagh K","Yee V","Lavik A","McColl K","Distelhorst CW"],"additional_accession":[]},"is_claimable":false,"name":"A Novel Peptide that Disrupts the Lck-IP<sub>3</sub>R Protein-Protein Interaction Induces Widespread Cell Death in Leukemia and Lymphoma.","description":"There is increasing evidence that the T-cell protein, Lck, is involved in the pathogenesis of chronic lymphocytic leukemia (CLL) as well as other leukemias and lymphomas. We previously discovered that Lck binds to domain 5 of inositol 1,4,5-trisphosphate receptors (IP<sub>3</sub>R) to regulate Ca<sup>2+</sup> homeostasis. Using bioinformatics, we targeted a region within domain 5 of IP<sub>3</sub>R-1 predicted to facilitate protein-protein interactions (PPIs). We generated a synthetic 21 amino acid peptide, KKRMDLVLELKNNASKLLLAI, which constitutes a domain 5 sub-domain (D5SD) of IP<sub>3</sub>R-1 that specifically binds Lck via its SH2 domain. With the addition of an HIV-TAT sequence to enable cell permeability of D5SD peptide, we observed wide-spread, Ca<sup>2+</sup>-dependent, cell killi","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023","modification":"2025-04-26T15:10:01.779Z","creation":"2024-11-21T09:48:19.787Z"},"accession":"S-EPMC10569261","cross_references":{"pubmed":["37829571"],"doi":["10.26502/ami.936500114"]}}