The Cooperative Effect between Polybasic Region (PBR) and Polysialyltransferase Domain (PSTD) within Tumor-Target Polysialyltranseferase ST8Sia II

Author(s): Guo-Ping Zhou*, Si-Ming Liao, Dong Chen, Ri-Bo Huang*.

Journal Name: Current Topics in Medicinal Chemistry

Volume 19 , Issue 31 , 2019

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Graphical Abstract:


Abstract:

ST8Sia II (STX) is a highly homologous mammalian polysialyltransferase (polyST), which is a validated tumor-target in the treatment of cancer metastasis reliant on tumor cell polysialylation. PolyST catalyzes the synthesis of α2,8-polysialic acid (polySia) glycans by carrying out the activated CMP-Neu5Ac (Sia) to N- and O-linked oligosaccharide chains on acceptor glycoproteins. In this review article, we summarized the recent studies about intrinsic correlation of two polybasic domains, Polysialyltransferase domain (PSTD) and Polybasic region (PBR) within ST8Sia II molecule, and suggested that the critical amino acid residues within the PSTD and PBR motifs of ST8Sia II for polysialylation of Neural cell adhesion molecules (NCAM) are related to ST8Sia II activity. In addition, the conformational changes of the PSTD domain due to point mutations in the PBR or PSTD domain verified an intramolecular interaction between the PBR and the PSTD. These findings have been incorporated into Zhou’s NCAM polysialylation/cell migration model, which will provide new perspectives on drug research and development related to the tumor-target ST8Sia II.

Keywords: Tumor metastasis, Polysialic acid (polySia), Polysialyltransferase domain (PSTD), Polybasic region (PBR), ST8Sia II (STX), ST8Sia IV (PST), Neural cell adhesion molecules (NCAM), Polysialylation, Protein 3D structure, Phyre2 sever.

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