期刊
CELL REPORTS
卷 22, 期 5, 页码 1151-1158出版社
CELL PRESS
DOI: 10.1016/j.celrep.2017.12.107
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资金
- National Natural Science Foundation of China [11574165]
- PCSIRT [IRT_13R29]
- 111 Project [B07013]
- Pew Biomedical Scholars Award
- Packard Fellowships for Science and Engineering
The erythrocyte cytoskeleton is a textbook prototype for the submembrane cytoskeleton of metazoan cells. While early experiments suggest a triangular network of actin-based junctional complexes connected by similar to 200-nm-long spectrin tetramers, later studies indicate much smaller junction-to-junction distances in the range of 25-60 nm. Through super-resolution microscopy, we resolve the native ultrastructure of the cytoskeleton of membrane-preserved erythrocytes for the N and C termini of b-spectrin, F-actin, protein 4.1, tropomodulin, and adducin. This allows us to determine an similar to 80-nm junction-to-junction distance, a length consistent with relaxed spectrin tetramers and theories based on spectrin abundance. Through two-color data, we further show that the cytoskeleton meshwork often contains nanoscale voids where the cell membrane remains intact and that actin filaments and capping proteins localize to a subset of, but not all, junctional complexes. Together, our results call for a reassessment of the structure and function of the submembrane cytoskeleton.
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