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KMID : 0578320100290040413
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Molecules and Cells
2010 Volume.29 No. 4 p.413 ~ p.418
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Tyrosylprotein Sulfotransferase Regulates Collagen Secretion in Caenorhabditis elegans
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Kim Tai-Hoon
Kim Do-Hyun
Nam Hyung-Wook
Park Sang-Yoon
Shim Jae-Gal
Cho Jin-Won
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Abstract
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The sulfation of tyrosine residues is an important post-translational modification involved in the regulation of protein function. We examined the activity of worm tyro-sylprotein sulfotransferase (TPST-1) on a typical cuticle collagen, ROL-6, in C. elegans. We verified that TPST-1 sulfates three tyrosine residues of ROL-6 in vitro. We found that these tyrosine residues are important for the secretion of ROL-6::GFP. Mutant ROL-6::GFP proteins that contain more than two substitutions of the target tyrosine residues are severely deficient in cuticle localization. Consistently, knock down of tpst-1 blocked the cuticle localization of ROL-6::GFP. Therefore, the sulfation of ROL-6 by TPST-1 is critical for the proper localization of ROL-6. We also confirmed that worm TPST-1 is localized to the trans-Golgi network (TGN). Our results indicate that TPST-1 regulates cuticle organi-zation by promoting the transport of ROL-6 from the TGN to the cuticle.
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KEYWORD
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C. elegans, collagen, protein sulfation, ROL-6, TPST-1
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