title: Membrane skeleton orchestrates the platelet glycoprotein (GP) Ib-IX complex clustering and signaling.
abstract: Platelet glycoprotein Ib-IX complex is affixed to the membrane skeleton through interaction with actin binding protein 280 (ABP-280). We find that removal of the ABP-280 binding sites in GP Ibα cytoplasmic tail has little impact on the complex clustering induced by antibody crosslinking. However, large truncation of the GP Ibα cytoplasmic tail allows the formation of larger patches of the complex, suggesting that an ABP-280 independent force may exist. Besides, we observe that the signaling upon GP Ib-IX clustering is elicited in both membrane lipid domain dependent and independent manner, a choice that relies on how the membrane skeleton interacts with the complex. Our findings suggest a more complex mechanism for how the membrane skeleton regulates the GP Ib-IX function. © 2016 IUBMB Life, 68(10):823-829, 2016.
authors.affiliation: Department of Vascular Surgery, Union Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, Hubei, China.|Department of Medicine, Cardiovascular Research Section, Baylor College of Medicine, Houston, TX.
authors.forename: Dan
authors.initials: D
authors.lastname: Shang
authors.affiliation: Department of Medicine, Cardiovascular Research Section, Baylor College of Medicine, Houston, TX.|Department of Parasitology, School of Basic Medicine, Central South University, Changsha, China.
authors.forename: Zuping
authors.initials: Z
authors.lastname: Zhang
authors.affiliation: Department of Medicine, Cardiovascular Research Section, Baylor College of Medicine, Houston, TX.
authors.forename: Qian
authors.initials: Q
authors.lastname: Wang
authors.affiliation: Department of Medicine, Cardiovascular Research Section, Baylor College of Medicine, Houston, TX.
authors.forename: Yali
authors.initials: Y
authors.lastname: Ran
authors.affiliation: Department of Medicine, Cardiovascular Research Section, Baylor College of Medicine, Houston, TX.
authors.forename: Tanner S
authors.initials: TS
authors.lastname: Shaw
authors.affiliation: Department of Medicine, Infectious Disease Section, Baylor College of Medicine, Houston, TX.
authors.forename: John N
authors.initials: JN
authors.lastname: Van
authors.affiliation: Department of Medicine, Cardiovascular Research Section, Baylor College of Medicine, Houston, TX. yuandong@bcm.edu.
authors.forename: Yuandong
authors.initials: Y
authors.lastname: Peng
mesh_terms: D002462:Cell Membrane / Q000378:metabolism*; D003599:Cytoskeleton / Q000378:metabolism; D006801:Humans; D020014:K562 Cells; D010766:Phosphorylation; D019038:Platelet Glycoprotein GPIb-IX Complex / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D015398:Signal Transduction
chemical_list: D019038:Platelet Glycoprotein GPIb-IX Complex
keywords: clustering; membrane lipid domain; membrane skeleton; platelet glycoprotein Ib-IX complex; signaling