Outer-arm dynein light chain LC1 is required for normal motor assembly kinetics, ciliary stability, and motility

• Published in: Molecular biology of the cell 2023-06, Vol.34 (7), p.ar75-ar75
• Main Authors: Sakato-Antoku, Miho, King, Stephen M
• Format: Article
• Language: English
• Subjects: Axonemal Dyneins - metabolism; Axoneme - metabolism; Chlamydomonas - metabolism; Cilia - metabolism; Dyneins - metabolism; Flagella - metabolism; Humans; Protein Binding; Transcription Factors - metabolism
• ISSN: 1059-1524; 1939-4586
• DOI: 10.1091/mbc.E23-03-0104

Light chain 1 (LC1) is a highly conserved leucine-rich repeat protein associated with the microtubule-binding domain of the outer-dynein arm γ heavy chain. LC1 mutations in humans and trypanosomes lead to motility defects, while its loss in oomycetes results in aciliate zoospores. Here we describe a LC1 null mutant ( ). This strain has reduced swimming velocity and beat frequency, can undergo waveform conversion, but often exhibits loss of hydrodynamic coupling between the cilia. Following deciliation, cells rapidly rebuild cytoplasmic stocks of axonemal dyneins. Loss of LC1 disrupts the kinetics of this cytoplasmic preassembly so that most outer-arm dynein heavy chains remain monomeric even after several hours. This suggests that association of LC1 with its heavy chain-binding site is a key step or checkpoint in the outer-arm dynein assembly process. Similarly to strains lacking the entire outer arm and inner arm I1/f, we found that loss of LC1 and I1/f in double mutants resulted in cells unable to build cilia under normal conditions. Furthermore, cells do not exhibit the usual ciliary extension in response to lithium treatment. Together, these observations suggest that LC1 plays an important role in the maintenance of axonemal stability.