A complex between phosphatidylinositol 4-kinase IIα and integrin α3β1 is required for N-glycan sialylation in cancer cells-Reference-Cited by-同舟云学术

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A complex between phosphatidylinositol 4-kinase IIα and integrin α3β1 is required for N-glycan sialylation in cancer cells

Published:2019-03 Issue:12 Volume:294 Page:4425-4436
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Isaji Tomoya,Im Sanghun,Kameyama Akihiko^ORCID,Wang Yuqin,Fukuda Tomohiko,Gu Jianguo

Funder

MEXT | Japan Society for the Promotion of Science

Ministry of Education, Culture, Sports, Science and Technology

NSFC | National Natural Science Foundation of China-Yunnan Joint Fund

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference88 articles.

1. ST6Gal-I expression in ovarian cancer cells promotes an invasive phenotype by altering integrin glycosylation and function;Christie;J. Ovarian Res,2008

2. Cell surface α2,6 sialylation affects adhesion of breast carcinoma cells;Lin;Exp. Cell Res,2002

3. Sialylation of β1 integrins blocks cell adhesion to galectin-3 and protects cells against galectin-3-induced apoptosis;Zhuo;J. Biol. Chem,2008

4. Structural and quantitative evidence of α2–6-sialylated N-glycans as markers of the differentiation potential of human mesenchymal stem cells;Hasehira;Glycoconj. J,2017

5. Glycosyltransferase ST6GAL1 contributes to the regulation of pluripotency in human pluripotent stem cells;Wang;Sci. Rep,2015

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