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http://dx.doi.org/10.5352/JLS.2020.30.1.10

Rab Effector EHBP1L1 Associates with the Tetratricopeptide Repeat Domain of Kinesin Light Chain 1  

Jeong, Young Joo (Departments of Biochemistry, Inje University College of Medicine)
Park, Sung Woo (Department of Convergence Biomedical Science, Inje University College of Medicine)
Kim, Sang-Jin (Department of Neurology, Inje University College of Medicine)
Kim, Mooseong (Department of Neurosurgery, Inje University College of Medicine)
Urm, Sang-Hwa (Department of Preventive Medicine, Inje University College of Medicine)
Lee, Jung Goo (Department of Psychiatry, College of Medicine, Haeundae Paik Hospital, Inje University)
Seog, Dae-Hyun (Departments of Biochemistry, Inje University College of Medicine)
Publication Information
Journal of Life Science / v.30, no.1, 2020 , pp. 10-17 More about this Journal
Abstract
Kinesin-1 is microtubule-dependent plus-end direct molecular motor protein essential for intracellular transport. It is a member of the kinesin superfamily proteins (KIFs) which transport cargo, including organelles, vesicles, neurotransmitter receptors, cell-signaling molecules, and protein complexes through interaction between its light chain subunit and the cargo. Kinesin light chain 1 (KLC1) is a non-motor subunit that associates with the kinesin heavy chain (KHC). Although KLC1 interacts with many different adaptor proteins and scaffolding proteins, its binding proteins have not yet been fully identified. We used the yeast two-hybrid assay to identify proteins that interact with the tetratricopeptide repeat (TPR) domain of KLC1, and found an interaction between KLC1 and EH domain-binding protein 1 like 1 (EHBP1L1). EHBP1L1 bound to the region containing all six TPR repeats of KLC1 and did not interact with KIF5B (a motor protein of kinesin 1) or KIF3A (a motor protein of kinesin 2) in the yeast two-hybrid assay. The carboxyl-terminus of the coiled-coil domain of EHBP1L1 is essential for interaction with KLC1. However, another EHBP1L1 isoform, EHBP1, did not interact with KLC1 in the yeast two-hybrid assay. KLC1 interacted with GST-EHBP1L1 and its coiled-coil domain but not with GST only. When co-expressed in HEK-293T cells, EHBP1L1 co-localized with KLC1 and co-immunoprecipitated with KLC1 and KIF5B but not KIF3A. These results suggest that kinesin 1 motor protein may transport EHBP1L1-associated cargo in cells.
Keywords
Adaptor protein; EHBP1L1; EH domain; kinesin 1; KLC1;
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