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Updated: Aug 12, 2026

Combined Nucleotide and Protein Extractions in Caenorhabditis elegans
Published on: March 17, 2019
Molecular and biochemical characterization of kettin in Caenorhabditis elegans
Shoichiro Ono1, Kurato Mohri, Kanako Ono
1Department of Pathology, Emory University, Whitehead Research Building, Atlanta, Georgia 30322, USA. sono@emory.edu
Abstract:
Kettin is a unique member of the connectin/titin family of muscle elastic proteins, which has repetitive immunoglobulin-like domains that are separated by weakly conserved linker sequences. In striated muscles of insects and crayfish, kettin binds to actin filaments and localizes to the Z-disc and its adjacent region in the I-band. Recent sequence analysis of invertebrate connectin/titin (also known as SLS proteins) has revealed that kettin is a splice variant of connectin/titin. In contrast, in the nematode Caenorhabditis elegans, the kettin gene is independent of the genes for other connectin/titin-related proteins. Immunofluorescent localization of kettin shows that it localizes to the I-bands in the obliquely striated body wall muscle. Therefore, C. elegans is an attractive model system to study specific functions of kettin in muscle cells.

