Juxtamembrane basic residues in glycoprotein Ibbeta cytoplasmic domain are required for assembly and surface expression of glycoprotein Ib-IX complex.
Platelet glycoprotein (GP) Ib-IX complex requires all its three subunits for efficient expression on the cell surface, but the underlying molecular basis is not fully clear. Using transfected Chinese hamster ovary cells as the model system, we demonstrate that juxtamembrane residues 149-154 in the cytoplasmic domain of the GPIbbeta subunit is required for assembly and surface expression of the GPIb-IX complex. The complex, or GPIbbeta by itself, lacking these residues is retained in the endoplasmic reticulum. Our results thus have illustrated an important role of the GPIbbeta cytoplasmic domain in biosynthesis of the GPIb-IX complex.
Mo
Xi
X
Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston, Houston, TX 77030, USA.
Luo
Shi-Zhong
SZ
López
José A
JA
Li
Renhao
R
D000595:Amino Acid Sequence; D000818:Animals; D016466:CHO Cells; D002462:Cell Membrane / Q000378:metabolism*; D006224:Cricetinae; D003412:Cricetulus; D003593:Cytoplasm / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation; D019038:Platelet Glycoprotein GPIb-IX Complex / Q000096:biosynthesis* / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary / Q000235:genetics; D014162:Transfection
D019038:Platelet Glycoprotein GPIb-IX Complex
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