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TMEM16F Forms a Ca2+-Activated Cation Channel Required for Lipid Scrambling in Platelets during Blood Coagulation
Open accessAbstract
SUMMARY Collapse of membrane lipid asymmetry is a hallmark of blood coagulation. TMEM16F of the TMEM16 family that includes TMEM16A/B Ca2+-activated Cl− channels (CaCCs) is linked to Scott syndrome with deficient Ca2+-dependent lipid scrambling. We generated TMEM16F knockout mice that exhibit bleeding defects and protection in an arterial thrombosis model associated with platelet deficiency in Ca2+-dependent phosphatidylserine exposure and procoagulant activity and lack a Ca2+-activated cation current in the platelet precursor megakaryocytes. Heterologous expression of TMEM16F generates a small-conductance Ca2+-activated nonselective cation (SCAN) current with subpicosiemens single-channel conductance rather than a CaCC. TMEM16F-SCAN channels permeate both monovalent and divalent cations, including Ca2+, and exhibit synergistic gating by Ca2+ and voltage. We further pinpointed a residue in the putative pore region important for the cation versus anion selectivity of TMEM16F-SCAN and TMEM16A-CaCC channels. This study thus identifies a Ca2+-activated channel permeable to Ca2+ and critical for Ca2+-dependent scramblase activity during blood coagulation.
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Cites
Mechanisms of Thrombus Formation
Furie, B., & Furie, B. C. (2008) · New England Journal of Medicine · doi:10.1056/nejmra0801082 · Cited by 1,926
Cited by
Exposure of phosphatidylserine on the cell surface
Nagata, S., Suzuki, J., Segawa, K., & Fujii, T. (2016) · Cell Death & Differentiation · doi:10.1038/cdd.2016.7 · Cited by 512
Getting to the Outer Leaflet: Physiology of Phosphatidylserine Exposure at the Plasma Membrane
Bevers, E. M., & Williamson, P. L. (2016) · Physiological Reviews · doi:10.1152/physrev.00020.2015 · Cited by 447
X-ray structure of a calcium-activated TMEM16 lipid scramblase
Brunner, J. D., Lim, N. K., Schenck, S., Duerst, A., & Dutzler, R. (2014) · Nature · doi:10.1038/nature13984 · Cited by 437
Structure-Guided Transformation of Channelrhodopsin into a Light-Activated Chloride Channel
Berndt, A., Lee, S. Y., Ramakrishnan, C., & Deisseroth, K. (2014) · Science · doi:10.1126/science.1252367 · Cited by 377
Platelet‐based coagulation: different populations, different functions
HEEMSKERK, J. W. M., MATTHEIJ, N. J. A., & COSEMANS, J. M. E. M. (2013) · Journal of Thrombosis and Haemostasis · doi:10.1111/jth.12045 · Cited by 370
Metadata
- Authors
- Yang, H., Kim, A., David, T., Palmer, D., Jin, T., Tien, J., Huang, F., Cheng, T., Coughlin, S. R., Jan, Y. N., & Jan, L. Y.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2012-09
- Volume
- 151
- Issue
- 1
- Pages
- 111-122
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2000178601
- Cited by
- 467
- References
- 1
- FWCI
- 22.09
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Yang, H., Kim, A., David, T., Palmer, D., Jin, T., Tien, J., Huang, F., Cheng, T., Coughlin, S. R., Jan, Y. N., & Jan, L. Y. (2012). TMEM16F Forms a Ca2+-Activated Cation Channel Required for Lipid Scrambling in Platelets during Blood Coagulation. Cell. https://doi.org/10.1016/j.cell.2012.07.036
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