Diverse roles of conserved asparagine-linked glycan sites on tyrosinase family glycoproteins Journal Article
| Authors: | Xu, Y.; Bartido, S.; Setaluri, V.; Qin, J.; Yang, G.; Houghton, A. N. |
| Article Title: | Diverse roles of conserved asparagine-linked glycan sites on tyrosinase family glycoproteins |
| Abstract: | The tyrosinase family of genes has been conserved throughout vertebrate evolution. The role of conserved N-glycan sites in sorting, stability, and activity of tyrosinase family proteins was investigated using two family members from two different species, mouse gp75/tyrosinase-related protein (TRP)-1/Tyrp1 and human tyrosinase. Potential N-linked glycosylation sites on the lumenal domains of mouse gp75/TRP-1/Tyrp1 and human tyrosinase were eliminated by site-directed mutagenesis (Asn to Gln substitutions). Our results show that selected conserved N-glycan sites on tyrosinase family members are crucial for stability in the secretory pathway and endocytic compartment and for enzymatic activity. Different glycan sites on the same tyrosinase family polypeptide can perform distinct functions, and conserved sites on tyrosinase family paralogues can perform different functions. © 2001 Academic Press. |
| Keywords: | controlled study; nonhuman; animal cell; mouse; animals; mice; amino acid substitution; protein targeting; protein stability; evolution; tumor cells, cultured; enzyme activity; vertebrata; amino acid sequence; conserved sequence; protein processing, post-translational; membrane glycoproteins; nucleotide sequence; protein transport; glycosylation; cell polarity; monophenol monooxygenase; polysaccharides; oxidoreductases; site directed mutagenesis; endocytosis; glycoproteins; glycoprotein; genetic conservation; glycan derivative; asparagine; multigene family; polypeptide; enzyme stability; tyrosinase; n-glycan; humans; priority journal; article; enzyme glycosylation; tyrosinase-related protein; protein sorting; asparagine derivative |
| Journal Title: | Experimental Cell Research |
| Volume: | 267 |
| Issue: | 1 |
| ISSN: | 0014-4827 |
| Publisher: | Elsevier Inc. |
| Date Published: | 2001-07-01 |
| Start Page: | 115 |
| End Page: | 125 |
| Language: | English |
| DOI: | 10.1006/excr.2001.5232 |
| PUBMED: | 11412044 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 21 May 2015 -- Source: Scopus |
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