-Galactoside 2,6-Sialyltransferase I Cleavage by BACE1 Enhances the Sialylation of Soluble Glycoproteins
نویسندگان
چکیده
Ichiro Sugimoto, Satoshi Futakawa, Ritsuko Oka, Kazuko Ogawa, Jamey D. Marth, Eiji Miyoshi , Naoyuki Taniguchi , Yasuhiro Hashimoto**, and Shinobu Kitazume From the Glyco-Chain Functions Laboratory, Institute of Physical and Chemical Research, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan, Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, Kawaguchi, Saitama 560-0082, Japan, the Department of Cellular and Molecular Medicine and the Howard Hughes Medical Institute, University of California, San Diego, La Jolla, California 92093, the Department of Biochemistry, Osaka University Graduate School of Medicine, Suita-shi, Osaka 565-871, Japan, and the **Department of Biochemistry, School of Medicine, Fukushima Medical University, Fukushima-shi, Fukushima 960-1295, Japan
منابع مشابه
Cleavage of ST6Gal I by Radiation-Induced BACE1 Inhibits Golgi-Anchored ST6Gal I-Mediated Sialylation of Integrin β1 and Migration in Colon Cancer Cells
BACKGROUND Previously, we found that β-galactoside α2,6-sialyltransferase (ST6Gal I), an enzyme that adds sialic acids to N-linked oligosaccharides of glycoproteins and is frequently overexpressed in cancer cells, is up-regulated by ionizing radiation (IR) and cleaved to a form possessing catalytic activity comparable to that of the Golgi-localized enzyme. Moreover, this soluble form is secrete...
متن کاملProtein sialylation by sialyltransferase involves radiation resistance.
Previously, we identified beta-galactoside alpha(2,6)-sialyltransferase (ST6Gal I) as a candidate biomarker for ionizing radiation. The expression of ST6Gal I and the level of protein sialylation increased following radiation exposure in a dose-dependent manner. Radiation induced ST6Gal I cleavage and the cleaved form of ST6Gal I was soluble and secreted. Sialylation of integrin beta1, a glycos...
متن کاملComplete switch from α-2,3- to α-2,6-regioselectivity in Pasteurella dagmatis β-D-galactoside sialyltransferase by active-site redesign.
Structure-guided active-site redesign of a family GT-80 β-D-galactoside sialyltransferase (from Pasteurella dagmatis) to change enzyme regioselectivity from α-2,3 in the wild type to α-2,6 in a P7H-M117A double mutant is reported. Biochemical data for sialylation of lactose together with protein crystal structures demonstrate highly precise enzyme engineering.
متن کاملThe 17-residue transmembrane domain of beta-galactoside alpha 2,6- sialyltransferase is sufficient for Golgi retention
beta-Galactoside alpha 2,6-sialyltransferase (ST) is a type II integral membrane protein of the Golgi apparatus involved in the sialylation of N-linked glycans. A series of experiments has shown that the 17-residue transmembrane domain of ST is sufficient to confer localization to the Golgi apparatus when transferred to the corresponding region of a cell surface type II integral membrane protei...
متن کاملStudies on the effect of lysosomotropic agents on the release of Galfl-4GlcNAc x-2,6-sialyltransferase from rat liver slices during the acute-phase response
The mechanism of release of Gal/31-4GlcNAc oc-2,6-sialyltransferase (CMP-N-acetylneuraminate: ,galactoside a-2,6-sialyltransferase, EC 2.4.99.1) from rat liver during the acute-phase response is due to the action of a cathepsin D-like proteinase that cleaves the trans-Golgi membrane-bound enzyme from a membrane anchor; this allows a major portion of the enzyme containing the catalytic site to e...
متن کامل