{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Vadla GP"],"funding":["NIH/NINDS","Missouri Spinal Cord Injury/Disease Research Program","Howard Hughes Medical Institute","NINDS NIH HHS","NIH","NIGMS NIH HHS"],"pagination":["e164608"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9977310"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(2)"],"pubmed_abstract":["SMA with respiratory distress type 1 (SMARD1) and Charcot-Marie-Tooth type 2S (CMT2S) are results of mutations in immunoglobulin mu DNA binding protein 2 (IGHMBP2). IGHMBP2 is a UPF1-like helicase with proposed roles in several cellular processes, including translation. This study examines activator of basal transcription 1 (ABT1), a modifier of SMARD1-nmd disease pathology. Microscale thermophoresis and dynamic light scattering demonstrate that IGHMBP2 and ABT1 proteins directly interact with high affinity. The association of ABT1 with IGHMBP2 significantly increases the ATPase and helicase activity as well as the processivity of IGHMBP2. The IGHMBP2/ABT1 complex interacts with the 47S pre-rRNA 5' external transcribed spacer and U3 small nucleolar RNA (snoRNA), suggesting that the IGHMBP2"],"journal":["JCI insight"],"pubmed_title":["ABT1 modifies SMARD1 pathology via interactions with IGHMBP2 and stimulation of ATPase and helicase activity."],"pmcid":["PMC9977310"],"funding_grant_id":["T32 GM008396","R01NS113765","Gilliam Fellowship","T32GM008396","R21NS103028","R21 NS109762","R01 NS113765","none","R21 NS103028"],"pubmed_authors":["Lorson ZC","Lorson CL","Singh K","Lorson MA","Rice RP","Hansen SA","Ricardez Hernandez SM","Vadla GP","Mao J","Garro-Kacher MO"],"additional_accession":[]},"is_claimable":false,"name":"ABT1 modifies SMARD1 pathology via interactions with IGHMBP2 and stimulation of ATPase and helicase activity.","description":"SMA with respiratory distress type 1 (SMARD1) and Charcot-Marie-Tooth type 2S (CMT2S) are results of mutations in immunoglobulin mu DNA binding protein 2 (IGHMBP2). IGHMBP2 is a UPF1-like helicase with proposed roles in several cellular processes, including translation. This study examines activator of basal transcription 1 (ABT1), a modifier of SMARD1-nmd disease pathology. Microscale thermophoresis and dynamic light scattering demonstrate that IGHMBP2 and ABT1 proteins directly interact with high affinity. The association of ABT1 with IGHMBP2 significantly increases the ATPase and helicase activity as well as the processivity of IGHMBP2. The IGHMBP2/ABT1 complex interacts with the 47S pre-rRNA 5' external transcribed spacer and U3 small nucleolar RNA (snoRNA), suggesting that the IGHMBP2","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jan","modification":"2025-04-04T20:09:51.25Z","creation":"2024-11-09T13:45:23.564Z"},"accession":"S-EPMC9977310","cross_references":{"pubmed":["36480289"],"doi":["10.1172/jci.insight.164608"]}}