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Structural Aspects of N-Glycosylations and the C-terminal Region in Human Glypican-1

Journal article
Authors W. Awad
Barbara Adamczyk
Jessica Örnros
Niclas G. Karlsson
K. Mani
D. T. Logan
Published in Journal of Biological Chemistry
Volume 290
Issue 38
Pages 22991-23008
ISSN 0021-9258
Publication year 2015
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 22991-23008
Language en
Links dx.doi.org/10.1074/jbc.M115.660878
Keywords x-ray-scattering, secondary structure prediction, heparan-sulfate, biological macromolecules, crystal-structure, core protein, web server, dally-like, glycans, cells, Biochemistry & Molecular Biology
Subject categories Biochemistry and Molecular Biology

Abstract

Glypicans are multifunctional cell surface proteoglycans involved in several important cellular signaling pathways. Glypican-1 (Gpc1) is the predominant heparan sulfate proteoglycan in the developing and adult human brain. The two N-linked glycans and the C-terminal domain that attach the core protein to the cell membrane are not resolved in the Gpc1 crystal structure. Therefore, we have studied Gpc1 using crystallography, small angle x-ray scattering, and chromatographic approaches to elucidate the composition, structure, and function of the N-glycans and the Cterminus and also the topology of Gpc1 with respect to the membrane. The Cterminus is shown to be highly flexible in solution, but it orients the core protein transverse to the membrane, directing a surface evolutionarily conserved in Gpc1 orthologs toward the membrane, where it may interact with signaling molecules and/or membrane receptors on the cell surface, or even the enzymes involved in heparan sulfate substitution in the Golgi apparatus. Furthermore, the N-glycans are shown to extend the protein stability and lifetime by protection against proteolysis and aggregation.

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