{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lee HS"],"funding":["National Research Foundation of Korea (NRF)","National Research Council of Science and Technology","Korea Research Institute of Bioscience and Biotechnology (KRIBB)","National Research Council of Science and Technology (NST)","National Research Foundation of Korea","Korea Research Institute of Bioscience and Biotechnology"],"pagination":["2945-2966"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12152161"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["26(11)"],"pubmed_abstract":["Microtubule-associated cargo transport, a central process governing the localization and movement of various cellular cargoes, is orchestrated by the coordination of two types of motor proteins (kinesins and dyneins), along with diverse adaptor and accessory proteins. Hook microtubule tethering protein 3 (Hook3) is a cargo adaptor that serves as a scaffold for recruiting kinesin family member 1C (KIF1C) and dynein, thereby regulating bidirectional cargo transport. Herein, we conduct structural and functional analyses of how Hook3 mediates KIF1C-dependent anterograde cargo transport through interaction with KIF1C and PTPN21. We verify the interactions among the three proteins and determine the crystal structure of the Hook3(553-624) - KIF1C(714-809) complex. Subsequent structure-based mutat"],"journal":["EMBO reports"],"pubmed_title":["Molecular basis for assembly and activation of the Hook3 - KIF1C complex-dependent transport machinery."],"pmcid":["PMC12152161"],"funding_grant_id":["CRC22021-700","KGM9952522","RS-2023-00278696","NRF-2022R1C1C200623113"],"pubmed_authors":["Do Heo W","Lee HS","Baek KE","Shin HC","Yu D","Kim SJ","Ku B"],"additional_accession":[]},"is_claimable":false,"name":"Molecular basis for assembly and activation of the Hook3 - KIF1C complex-dependent transport machinery.","description":"Microtubule-associated cargo transport, a central process governing the localization and movement of various cellular cargoes, is orchestrated by the coordination of two types of motor proteins (kinesins and dyneins), along with diverse adaptor and accessory proteins. Hook microtubule tethering protein 3 (Hook3) is a cargo adaptor that serves as a scaffold for recruiting kinesin family member 1C (KIF1C) and dynein, thereby regulating bidirectional cargo transport. Herein, we conduct structural and functional analyses of how Hook3 mediates KIF1C-dependent anterograde cargo transport through interaction with KIF1C and PTPN21. We verify the interactions among the three proteins and determine the crystal structure of the Hook3(553-624) - KIF1C(714-809) complex. Subsequent structure-based mutat","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jun","modification":"2026-06-03T06:03:16.369Z","creation":"2026-05-29T03:05:58.687Z"},"accession":"S-EPMC12152161","cross_references":{"pubmed":["40312563"],"doi":["10.1038/s44319-025-00458-w"]}}