Warning: Undefined variable $zfal in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 525
Deprecated: str_replace(): Passing null to parameter #3 ($subject) of type array|string is deprecated in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 525
Warning: Undefined variable $sterm in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 530
Warning: Undefined variable $sterm in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 531
English Wikipedia
Nephropedia Template TP (
Twit Text
DeepDyve Pubget Overpricing |
lüll Lectins and traffic in the secretory pathway Hauri H; Appenzeller C; Kuhn F; Nufer OFEBS Lett 2000[Jun]; 476 (1-2): 32-7Evidence is accumulating that intracellular animal lectins play important roles in quality control and glycoprotein sorting along the secretory pathway. Calnexin and calreticulin in conjunction with associated chaperones promote correct folding and oligomerization of many glycoproteins in the endoplasmic reticulum (ER). The mannose lectin ERGIC-53 operates as a cargo receptor in transport of glycoproteins from ER to Golgi and the homologous lectin VIP36 may operate in quality control of glycosylation in the Golgi. Exit from the Golgi of lysosomal hydrolases to endosomes requires mannose 6-phosphate receptors and exit to the apical plasma membrane may also involve traffic lectins. Here we discuss the features of these lectins and their role in glycoprotein traffic in the secretory pathway.|Amino Acid Sequence[MESH]|Animals[MESH]|Calcium-Binding Proteins/*metabolism[MESH]|Calnexin[MESH]|Calreticulin[MESH]|Glycoproteins/*metabolism[MESH]|Humans[MESH]|Lectins/chemistry/*metabolism[MESH]|Molecular Chaperones/metabolism[MESH]|Protein Folding[MESH]|Ribonucleoproteins/*metabolism[MESH]|Saccharomyces cerevisiae/metabolism[MESH]|Sequence Alignment[MESH]|Sequence Homology, Amino Acid[MESH] |