Molecular and biochemical characterization of kettin in Caenorhabditis elegans.
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.
Ono
Shoichiro
S
Department of Pathology, Emory University, Whitehead Research Building, Atlanta, Georgia 30322, USA. sono@emory.edu
Mohri
Kurato
K
Ono
Kanako
K
D000199:Actins / Q000378:metabolism; D000818:Animals; D015153:Blotting, Western; D017173:Caenorhabditis elegans / Q000235:genetics / Q000378:metabolism*; D029742:Caenorhabditis elegans Proteins / Q000235:genetics / Q000378:metabolism*; D064211:Connectin; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics; D008840:Microfilament Proteins / Q000235:genetics / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D009124:Muscle Proteins / Q000235:genetics / Q000378:metabolism*; D009132:Muscles / Q000378:metabolism; D009210:Myofibrils / Q000378:metabolism; D017422:Sequence Analysis, DNA; D016596:Vinculin / Q000378:metabolism
D000199:Actins; D029742:Caenorhabditis elegans Proteins; D064211:Connectin; D018076:DNA, Complementary; D008840:Microfilament Proteins; D009124:Muscle Proteins; C577345:ketn-1 protein, C elegans; D016596:Vinculin