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Title | The protein organization of a red blood cell. |
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Journal, issue, pages | Cell Rep, Vol. 40, Issue 3, Page 111103, Year 2022 |
Publish date | Jul 19, 2022 |
Authors | Wisath Sae-Lee / Caitlyn L McCafferty / Eric J Verbeke / Pierre C Havugimana / Ophelia Papoulas / Claire D McWhite / John R Houser / Kim Vanuytsel / George J Murphy / Kevin Drew / Andrew Emili / David W Taylor / Edward M Marcotte / |
PubMed Abstract | Red blood cells (RBCs) (erythrocytes) are the simplest primary human cells, lacking nuclei and major organelles and instead employing about a thousand proteins to dynamically control cellular ...Red blood cells (RBCs) (erythrocytes) are the simplest primary human cells, lacking nuclei and major organelles and instead employing about a thousand proteins to dynamically control cellular function and morphology in response to physiological cues. In this study, we define a canonical RBC proteome and interactome using quantitative mass spectrometry and machine learning. Our data reveal an RBC interactome dominated by protein homeostasis, redox biology, cytoskeletal dynamics, and carbon metabolism. We validate protein complexes through electron microscopy and chemical crosslinking and, with these data, build 3D structural models of the ankyrin/Band 3/Band 4.2 complex that bridges the spectrin cytoskeleton to the RBC membrane. The model suggests spring-like compression of ankyrin may contribute to the characteristic RBC cell shape and flexibility. Taken together, our study provides an in-depth view of the global protein organization of human RBCs and serves as a comprehensive resource for future research. |
External links | Cell Rep / PubMed:35858567 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.4 Å |
Structure data | EMDB-24822: 20S proteasome from red blood cell lysate |
Source |
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