Dynein light chains 1 and 2 are auxiliary proteins of pH-sensitive Kir4.1 channels.

ABSTRACT: Inward rectifier Kir4.1 potassium channels are abundantly expressed in cells that are important for electrolyte homeostasis. Dysregulation of Kir4.1 underlies various neurological disorders. Here, through biochemical and structural studies of full-length Kir4.1, we show that dynein light chain 1 and 2 proteins, also as known as LC8, copurify with Kir4.1 at stoichiometric levels. Direct interaction between Kir4.1 and LC8 is supported by in vitro binding assays and reiterated with native Kir4.1 proteins from mouse brain. Notably, we identify a LC8 binding motif in the unstructured N terminus of Kir4.1. Among Kir subtypes, the motif is unique to Kir4.1 and is highly conserved between Kir4.1 orthologs. Deletion of the predicted anchoring sequence (ΔTQT) resulted in loss of LC8 interaction with

SUBMITTER: Lee SJ 

PROVIDER: S-EPMC11999606 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature