Intracellular lectins associated with N-linked glycoprotein traffic

• Published in: BBA - General Subjects Vol. 1473; no. 1; pp. 147 - 160
• Main Authors: Yamashita, Katsuko, Hara-Kuge, Sayuri, Ohkura, Takashi
• Format: Book Review Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 06.12.1999
• Subjects: Animals; Apical traffic; Biological Transport; Calcium-Binding Proteins - metabolism; Calnexin; Calreticulin; Carbohydrate Sequence; Carrier Proteins - metabolism; Cell Membrane - metabolism; Endoplasmic Reticulum - metabolism; Endoplasmic reticulum-Golgi intermediate compartment; Epithelial Cells - metabolism; Glycoproteins - metabolism; Golgi Apparatus - metabolism; Lectins - metabolism; Mannose 6-phosphate; Mannose-Binding Lectins; Membrane Proteins - metabolism; Molecular Sequence Data; N-Linked glycan; Ribonucleoproteins - metabolism; Vesicular integral protein of 36 kDa; VIP, vesicular integral membrane protein; FRT, Fischer rat thyroid; GST, glutathione S-transferase; MDCK, Madin-Darby canine kidney; CEA, carcinoembryonic antigen; TGN, trans-Golgi network; GPI, glycosylphosphatidylinositol; Calnexin; COP, coat protein; IGF-II, insulin-like growth factor-II; Mannose 6-phosphate; CD, cation-dependent; Vesicular integral protein of 36 kDa; MR60, mannose-specific membrane lectin; THP, Tamm-Horsfall glycoprotein; Endoplasmic reticulum-Golgi intermediate compartment; ERGIC, ER-Golgi intermediate compartment; PNS, post-nuclear supernatant; Apical traffic; ERp57, endoplasmic reticulum protein of 57 kDa; M6P, mannose 6-phosphate; ER, endoplasmic reticulum; N-Linked glycan
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/S0304-4165(99)00175-0

The vectorial intracellular transport of N-glycan-linked glycoproteins is indispensable for biological functions. In order to sort these glycoproteins to the correct destination, animal intracellular lectins play important roles as sorting receptors. The roles of such lectins in the biosynthetic pathway from the endoplasmic reticulum (ER) to the cell surface are addressed in this review. Calnexin and calreticulin function via specific carbohydrates in quality control of newly synthesized glycoproteins in the ER, and ERGIC-53 seems to function in the transport of glycoproteins from ER to the Golgi complex. In addition to the well-understood role of mannose 6-phosphate receptor in lysosomal protein sorting, the vesicular integral protein of 36 kDa (VIP36) functions as a sorting receptor by recognizing high-mannose type glycans containing α1→2Man residues for transport from Golgi to the cell surface in polarized epithelial cells.