Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8384014 | FEBS Letters | 2008 | 5 Pages |
Abstract
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 GPIbβ subunit is required for assembly and surface expression of the GPIb-IX complex. The complex, or GPIbβ by itself, lacking these residues is retained in the endoplasmic reticulum. Our results thus have illustrated an important role of the GPIbβ cytoplasmic domain in biosynthesis of the GPIb-IX complex.Structured summaryMINT-6742751, MINT-6742907:GPIX (uniprotkb:P14770), GPIbalpha (uniprotkb:P07359)and GPIbbeta (uniprotkb:P13224) physically interact (MI:0218) by fluorescence-activated cell sorting (MI:0054)
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Xi Mo, Shi-Zhong Luo, José A. López, Renhao Li,