Tyrosylprotein sulfotransferase regulates collagen secretion in Caenorhabditis elegans.

Tai Hoon Kim, Do Hyun Kim, Hyung Wook Nam, Sang Yoon Park, Jaegal Shim, Jin Won Cho

Research output: Contribution to journalArticle

7 Citations (Scopus)


The sulfation of tyrosine residues is an important post-translational modification involved in the regulation of protein function. We examined the activity of worm tyrosylprotein 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 organization by promoting the transport of ROL-6 from the TGN to the cuticle.

Original languageEnglish
Pages (from-to)413-418
Number of pages6
JournalMolecules and cells
Issue number4
Publication statusPublished - 2010 Apr

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

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