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Published on: October 2, 2017
Structural and biochemical studies of the extracellular domain of Myelin protein zero-like protein 1
Tianshu Yu1, Ling Liang2, Xuyang Zhao3
1Peking-Tsinghua Center for Life Sciences, Peking University, Beijing, 100871, China.
Insights
Myelin protein zero-like protein 1 (MPZL1) binds concanavalin A (ConA) via glycosylation at Asn50. This interaction and MPZL1 dimerization are crucial for hepatocellular carcinoma (HCC) cell migration.
Area of Science:
- Biochemistry
- Molecular Biology
- Cancer Research
Background:
- Myelin protein zero-like protein 1 (MPZL1) is implicated in hepatocellular carcinoma (HCC) progression.
- The precise function of MPZL1 as a concanavalin A (ConA) receptor and its role in HCC remain unclear.
Purpose of the Study:
- To elucidate the structural and functional basis of MPZL1's interaction with ConA.
- To investigate the role of MPZL1 glycosylation and dimerization in HCC.
Main Methods:
- X-ray crystallography was used to determine the structure of the extracellular domain of MPZL1.
- Analysis of glycosylation sites and protein-protein interactions (homodimerization).
Main Results:
- The crystal structure revealed MPZL1 folds as an immunoglobulin variable-like domain.
- Asn50 was identified as a unique glycosylation site essential for ConA binding.
- MPZL1 forms homodimers in the crystal, stabilized by hydrogen bonds involving Ser86 and Val145.
Conclusions:
- Glycosylation of Asn50 is critical for MPZL1's function as a ConA receptor.
- MPZL1 dimerization likely plays a role in regulating signal transduction in cell adhesion processes relevant to HCC.
Abstract:
Myelin protein zero-like protein 1 (MPZL1) is a member of the immunoglobulin superfamily, and is also a receptor of concanavalin A (ConA). MPZL1 is upregulated in hepatocellular carcinoma (HCC) and accelerates migration of HCC cells. However, function of MPZL1 as a receptor of ConA and its role in HCC development are largely unknown. To elucidate the functional basis, we have determined the crystal structure of the extracellular domain of MPZL1 at 2.7 Å resolution. Overall, it folds like a typical immunoglobulin variable-like domain that is much like MPZ. Unexpectedly, we found Asn50 is a unique glycosylation site and the glycosylation mediates its interaction with ConA. Furthermore, we also found that MPZL1 exists as a homodimer in the crystal, in which hydrogen bonds between Ser86 and Val145 play an important role. Our results demonstrate that glycosylation of Asn50 is essential for its function as a receptor of ConA. We propose that dimerization of MPZL1 participates in control of its signal transmission in cell adhesion.
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