Published 9 July 2001. doi:10.1083/jcb.200106072
© The Rockefeller University Press,
0021-9525/2001/7/21 $5.00
The Journal of Cell Biology, Volume 154, Number 1, July 9, 2001 21-24
Fishing out proteins that bind to titin
Joseph W. Sanger and
Jean M. Sanger
Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104
Address correspondence to Joseph W. Sanger, Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6058. Tel.: (215) 898-6919. Fax: (215) 898-9871. E-mail: sangerj{at}mail.med.upenn.edu
Another giant protein has been detected in cross-striated muscle cells. Given the name obscurin, it was discovered in a yeast two-hybrid screen in which the bait was a small region of titin that is localized near the Z-band. Obscurin is about 720 kD, similar in molecular weight to nebulin, but present at about one tenth the level (Young et al., 2001). Like titin, obscurin contains multiple immunoglobulin-like domains linked in tandem, but in contrast to titin it contains just two fibronectin-like domains. It also contains sequences that suggest obscurin may have roles in signal transduction. During embryonic development, its localization changes from the Z-band to the M-band. With these intriguing properties, obscurin may not remain obscure for long.
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