Dejima Katsufumi
   Department   School of Medicine, School of Medicine
   Position   Assistant Professor
Article types Original article
Language English
Peer review Peer reviewed
Title Two Golgi-resident 3'-Phosphoadenosine 5'-phosphosulfate transporters play distinct roles in heparan sulfate modifications and embryonic and larval development in Caenorhabditis elegans.
Journal Formal name:The Journal of biological chemistry
Abbreviation:J Biol Chem
ISSN code:1083-351X(Electronic)0021-9258(Linking)
Volume, Issue, Page 285(32),24717-28頁
Author and coauthor Dejima Katsufumi, Murata Daisuke, Mizuguchi Souhei, Nomura Kazuko H, Izumikawa Tomomi, Kitagawa Hiroshi, Gengyo-Ando Keiko, Yoshina Sawako, Ichimiya Tomomi, Nishihara Shoko, Mitani Shohei, Nomura Kazuya
Publication date 2010/08
Summary Synthesis of extracellular sulfated molecules requires active 3'-phosphoadenosine 5'-phosphosulfate (PAPS). For sulfation to occur, PAPS must pass through the Golgi membrane, which is facilitated by Golgi-resident PAPS transporters. Caenorhabditis elegans PAPS transporters are encoded by two genes, pst-1 and pst-2. Using the yeast heterologous expression system, we characterized PST-1 and PST-2 as PAPS transporters. We created deletion mutants to study the importance of PAPS transporter activity. The pst-1 deletion mutant exhibited defects in cuticle formation, post-embryonic seam cell development, vulval morphogenesis, cell migration, and embryogenesis. The pst-2 mutant exhibited a wild-type phenotype. The defects observed in the pst-1 mutant could be rescued by transgenic expression of pst-1 and hPAPST1 but not pst-2 or hPAPST2. Moreover, the phenotype of a pst-1;pst-2 double mutant were similar to those of the pst-1 single mutant, except that larval cuticle formation was more severely defected. Disaccharide analysis revealed that heparan sulfate from these mutants was undersulfated. Gene expression reporter analysis revealed that these PAPS transporters exhibited different tissue distributions and subcellular localizations. These data suggest that pst-1 and pst-2 play different physiological roles in heparan sulfate modification and development.
DOI 10.1074/jbc.M109.088229
Document No. 20529843