Glycometabolome Team
Team Leader
Tadashi SUZUKI (D.Sci.)
Peptide:N-glycanase (PNGase) releases N-glycans from glycoproteins/glycopeptides. The cytoplasmic PNGases, ubiquitously found throughout eukaryotes, are now widely recognized as a component implicated in the ERAD (ER-associated degradation) process, which constitute one of the quality control machineries for newly synthesized misfolded glycoproteins exported out of the ER lumen. While the biosynthetic pathway for N-glycans has been clarified in detail, the catabolic pathway for the "free" N-glycans released by the cytoplasmic PNGase remains largrely unknown. Although this "non-lysosomal" metabolic path for N-glycan may represent one of the very basic biological phenomena in eukaryotes, there are still many more enzymes/transporters that remains to be identified.. We are currently trying to identify other players involved in this process, and also taking a number of approaches to analyze the physiological importance of this non-lysosomal metabolic pathway.
- Mechanism of free N-glycan catabolic pathway
- Functional role of cytoplasmic PNGase in ERAD
- Evolutional Diversion of the function of cytoplasmic PNGase
- May 31, 2010
- Diversity discovered in mechanisms for degrading poorly-formed abnormal glycoproteins
- May 11, 2010
- New function for degrading poorly-formed proteins discovered in PNGase
- February 18, 2010
- New catabolic pathway proposed for the decomposition of abnormal glycoproteins
- Hosomi, A., Tanabe, K., Hirayama, H., Kim, I., Rao, H., and Suzuki, T.:
"Identification of an Htm1 (EDEM)-dependent, Mns1-independent endoplasmic reticulum-associated degradation (ERAD) pathway in Saccharomyces cerevisiae. Application of a novel assay for glycoprotein ERAD."
J. Biol. Chem. 285, 24324-24334 (2010) - Funakoshi, Y., Negishi, Y., Gergen, J. P., Seino, J., Ishii, K., Lennarz, W.J., Matsuo, I., Ito, Y., Taniguchi, N., and Suzuki, T..:
"Evidence for an essential deglycosylation-independent activity of PNGase in Drosophila melanogaster."
PLoS One, 5, e10545 (2010) - Hirayama, H., Seino, J., Kitajima, T., Jigami, Y., and Suzuki, T.:
"Free oligosaccharides to monitor glycoprotein endoplasmic reticulum-associated degradation in Saccharomyces cerevisiae."
J. Biol. Chem. 285, 12390-12404 (2010) - Maerz, S., Funakoshi, Y., Negishi, Y., Suzuki, T., and Seiler, S.:
"The Neurospora peptide:N-glycanase ortholog PNG1 is essential for cell polarity despite its lack of enzymatic activity."
J. Biol. Chem. 285, 2326-2332 (2010) - Haga, Y., Totani, K., Ito, Y., and Suzuki, T.:
"Establishment of a real-time analytical method for free oligosaccharide transport from the ER to the cytosol."
Glycobiology 19, 987-994 (2009) - Funakoshi, Y and Suzuki, T.:
"Glycobiology in the cytosol: the bitter side of a sweet world."
Biochim. Biophys. Acta 1790, 81-94 (2009) - Suzuki, T., Matsuo, I., Totani, K., Funayama, S., Seino, J., Taniguchi, N., Ito, Y., and Hase, S.:
"Dual-gradient HPLC for identification of cytosolic high mannose-type free glycans."
Anal. Biochem. 381, 224-232 (2008) - Ishizuka, A., Hashimoto, Y., Naka, R., Kinoshita, M., Kakehi, K#., Seino, J., Funakoshi, Y., Suzuki, T#., Kameyama, A., and Narimatsu, H. (#, corresponding authors):
"Cytoplasmic peptide:N-glycanase and catabolic pathway for free N-glycans in the cytosol."
Biochem. J. 413, 227-237 (2008) - Suzuki, T.:
"Cytoplasmic peptide:N-glycanase and catabolic pathway for free N-glycans in the cytosol."
Sem. Cell Develop. Biol. 18, 762-769 (2007) - Suzuki, T., Hara, I., Nakano, M., Zhao, G., Lennarz, W. J., Schindelin, H., Totani, K., Matsuo, I., and Ito, Y.:
"Site-specific labeling of cytoplasmic peptide:N-glycanase by N,N'-diacetylchitobiose-related compounds."
J. Biol. Chem. 281, 22152-22160 (2006)