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Cleavage and phosphorylation: important post-translational modifications of galectin-3

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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.

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  1. Xiaoge Gao, Jingjie Liu contributed equally to this work.

Authors and Affiliations

  1. Cancer Institute, Xuzhou Medical University, Xuzhou, Jiangsu Province, 221002, People’s Republic of China

    Xiaoge Gao, Jingjie Liu, Liantao Li & Junnian Zheng

  2. 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

    Xiangye Liu

  3. Center of Clinical Oncology, Affiliated Hospital of Xuzhou Medical University, Xuzhou, Jiangsu Province, 221002, People’s Republic of China

    Liantao Li & Junnian Zheng

  4. Jiangsu Center for the Collaboration and Innovation of Cancer Biotherapy, Cancer Institute, Xuzhou Medical University, Xuzhou, Jiangsu Province, 221002, People’s Republic of China

    Junnian Zheng

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  1. Xiaoge Gao
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Correspondence to Junnian Zheng.

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This work was supported by the National Natural Science Foundation of China (Grant No. 81502221), the China Postdoctoral Science Foundation (Grant No. 2016M590504), and the Natural Science Foundation of Jiangsu Province (Grant No. BK20150216, BK20161157), the Jiangsu Province Postdoctoral Science Foundation (Grant No. 1501088B), and the Research Foundation of Xuzhou Medical University (Grant No. D2015009).

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Gao, X., Liu, J., Liu, X. et al. Cleavage and phosphorylation: important post-translational modifications of galectin-3. Cancer Metastasis Rev 36, 367–374 (2017). https://doi.org/10.1007/s10555-017-9666-0

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