title: Cleavage and phosphorylation: important post-translational modifications of galectin-3.
abstract: As the unique chimeric member of the β-galactoside-binding protein family, galectin-3 is a multivalent and multifunctional oncogenic protein involved in multiple physiological and pathological processes, including cell growth, cell differentiation, cell adhesion, RNA splicing, cell apoptosis, and malignant transformation. Post-translational modifications can effectively increase a protein's functional diversity, either by degradation or adding chemical modifications, thus regulating activity, localization, and ligand interaction. In order to clearly understand the functional mechanisms of galectin-3 involved in normal cell biology and pathogenesis, here, we have summarized the previously reported post-translational modifications of galectin-3, including cleavage and phosphorylation. Cleavage of galectin-3 by MMPs, PSA, and proteases from parasites generated intact carbohydrate-recognition domain and N-terminal peptides of varying lengths that retained lectin binding activity but lost multivalence. Serine and tyrosine phosphorylation of galectin-3 by c-Abl, CKI, and GSK-3β could regulate its localization and associated signal transduction. Accordingly, cleavage and phosphorylation play an important role in regulating galectin-3 function via altering its multivalence, localization, and ligand interaction.
authors.affiliation: Cancer Institute, Xuzhou Medical University, Xuzhou, Jiangsu Province, 221002, People's Republic of China.
authors.forename: Xiaoge
authors.initials: X
authors.lastname: Gao
authors.affiliation: Cancer Institute, Xuzhou Medical University, Xuzhou, Jiangsu Province, 221002, People's Republic of China.
authors.forename: Jingjie
authors.initials: J
authors.lastname: Liu
authors.affiliation: Jiangsu Province Key Laboratory of Immunity and Metabolism, Department of Pathogenic Biology and Immunology, Xuzhou Medical University, Xuzhou, Jiangsu Province, 221004, People's Republic of China.
authors.forename: Xiangye
authors.initials: X
authors.lastname: Liu
authors.affiliation: Cancer Institute, Xuzhou Medical University, Xuzhou, Jiangsu Province, 221002, People's Republic of China.|Center of Clinical Oncology, Affiliated Hospital of Xuzhou Medical University, Xuzhou, Jiangsu Province, 221002, People's Republic of China.
authors.forename: Liantao
authors.initials: L
authors.lastname: Li
authors.affiliation: Cancer Institute, Xuzhou Medical University, Xuzhou, Jiangsu Province, 221002, People's Republic of China. jnzheng@xzhmu.edu.cn.|Center of Clinical Oncology, Affiliated Hospital of Xuzhou Medical University, Xuzhou, Jiangsu Province, 221002, People's Republic of China. jnzheng@xzhmu.edu.cn.|Jiangsu Center for the Collaboration and Innovation of Cancer Biotherapy, Cancer Institute, Xuzhou Medical University, Xuzhou, Jiangsu Province, 221002, People's Republic of China. jnzheng@xzhmu.edu.cn.
authors.forename: Junnian
authors.initials: J
authors.lastname: Zheng
mesh_terms: D000818:Animals; D037502:Galectin 3 / Q000378:metabolism*; D006801:Humans; D020782:Matrix Metalloproteinases / Q000378:metabolism; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational
chemical_list: D037502:Galectin 3; D020782:Matrix Metalloproteinases
keywords: Cleavage; Function; Galectin-3; Multivalence; Phosphorylation