Requirement of tyrosylprotein sulfotransferase-A for proper cuticle formation in the nematode C. elegans

Tai Hoon Kim, Soon Baek Hwang, Pan Young Jeong, Junho Lee, Jin Won Cho

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Tyrosine O-sulfation is one of the post-translational modification processes that occur to membrane proteins and secreted proteins in eukaryotes. Tyrosylprotein sulfotransferase (TPST) is responsible for this modification, and in this report, we describe the expression pattern and the biological role of TPST-A in the nematode Caenorhabditis elegans. We found that TPST-A was mainly expressed in the hypodermis, especially in the seam cells. Reduction of TPST-A activity by RNAi caused severe defects in cuticle formation, indicating that TPST-A is involved in the cuticle formation in the nematode. We found that RNAi of TPST-A suppressed the roller phenotype caused by mutations in the rol-6 collagen gene, suggesting that sulfation of collagen proteins may be important for proper organization of the extracellular cuticle matrix. The TPST-A RNAi significantly decreased the dityrosine level in the worms, raising the possibility that the sulfation process may be a pre-requisite for the collagen tyrosine cross-linking.

Original languageEnglish
Pages (from-to)53-58
Number of pages6
JournalFEBS Letters
Volume579
Issue number1
DOIs
Publication statusPublished - 2005 Jan 3

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Molecular Biology

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