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Membrane skeleton orchestrates the platelet glycoprotein (GP) Ib‐IX complex clustering and signaling
Author(s) -
Shang Dan,
Zhang Zuping,
Wang Qian,
Ran Yali,
Shaw Tanner S.,
Van John N.,
Peng Yuandong
Publication year - 2016
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.1559
Subject(s) - cytoplasm , microbiology and biotechnology , glycoprotein , membrane glycoproteins , platelet , biology , membrane , function (biology) , chemistry , biochemistry , immunology
Summary 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 The Authors IUBMB Life published by Wiley Periodicals, Inc. on behalf of International Union of Biochemistry and Molecular Biology, 68(10):823–829, 2016