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A posttranslational modification of beta-actin contributes to the slow dissociation of the spectrin-protein 4.1-actin complex of irreversibly sickled cells.
J Cell Biol. 1995 Mar; 128(5):805-18.JC

Abstract

Irreversibly sickled cells (ISCs) remain sickled even under conditions where they are well oxygenated and hemoglobin is depolymerized. In our studies we demonstrate that triton extracted ISC core skeletons containing only spectrin, protein 4.1, and actin also retain their sickled shape; while reversibly sickled cell (RSC) skeletons remodel to a round or biconcave shape. We also demonstrate that these triton extracted ISC core skeletons dissociate more slowly upon incubation at 37 degrees C than do RSC or control (AA) core skeletons. This observation may supply the basis for the inability of the ISC core skeleton to remodel its shape. Using an in vitro ternary complex dissociation assay, we demonstrate that a modification in beta-actin is the major determinant of the slow dissociation of the spectrin-protein 4.1-actin complex isolated from the ISC core skeleton. We demonstrate that the difference between ISC and control beta-actin is the inaccessibility of two cysteine residues in ISC beta-actin to labeling by thiol reactive reagents; due to the formation of a disulfide bridge between cysteine284 and cysteine373 in ISC beta-actin, or alternatively another modification of cysteine284 and cysteine373 which is reversible with DTT and adds less than 100 D to the molecular weight of beta-actin.

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Authors+Show Affiliations

Shartava A
Department of Structural and Cellular Biology, University of South Alabama College of Medicine, Mobile 36688.
Monteiro CA
No affiliation info available
Bencsath FA
No affiliation info available
Schneider K
No affiliation info available
Chait BT
No affiliation info available
Gussio R
No affiliation info available
Casoria-Scott LA
No affiliation info available
Shah AK
No affiliation info available
Heuerman CA
No affiliation info available
Goodman SR
No affiliation info available

MeSH

ActinsAmino Acid SequenceAnemia, Sickle CellComputer SimulationCytoskeletal ProteinsErythrocyte MembraneErythrocytes, AbnormalHumansMacromolecular SubstancesMass SpectrometryMembrane ProteinsModels, MolecularMolecular Sequence DataNeuropeptidesProtein BindingProtein Processing, Post-TranslationalSequence AnalysisSpectrin

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

7876306

Citation

Shartava, A, et al. "A Posttranslational Modification of Beta-actin Contributes to the Slow Dissociation of the Spectrin-protein 4.1-actin Complex of Irreversibly Sickled Cells." The Journal of Cell Biology, vol. 128, no. 5, 1995, pp. 805-18.
Shartava A, Monteiro CA, Bencsath FA, et al. A posttranslational modification of beta-actin contributes to the slow dissociation of the spectrin-protein 4.1-actin complex of irreversibly sickled cells. J Cell Biol. 1995;128(5):805-18.
Shartava, A., Monteiro, C. A., Bencsath, F. A., Schneider, K., Chait, B. T., Gussio, R., Casoria-Scott, L. A., Shah, A. K., Heuerman, C. A., & Goodman, S. R. (1995). A posttranslational modification of beta-actin contributes to the slow dissociation of the spectrin-protein 4.1-actin complex of irreversibly sickled cells. The Journal of Cell Biology, 128(5), 805-18.
Shartava A, et al. A Posttranslational Modification of Beta-actin Contributes to the Slow Dissociation of the Spectrin-protein 4.1-actin Complex of Irreversibly Sickled Cells. J Cell Biol. 1995;128(5):805-18. PubMed PMID: 7876306.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A posttranslational modification of beta-actin contributes to the slow dissociation of the spectrin-protein 4.1-actin complex of irreversibly sickled cells. AU - Shartava,A, AU - Monteiro,C A, AU - Bencsath,F A, AU - Schneider,K, AU - Chait,B T, AU - Gussio,R, AU - Casoria-Scott,L A, AU - Shah,A K, AU - Heuerman,C A, AU - Goodman,S R, PY - 1995/3/1/pubmed PY - 1995/3/1/medline PY - 1995/3/1/entrez SP - 805 EP - 18 JF - The Journal of cell biology JO - J Cell Biol VL - 128 IS - 5 N2 - Irreversibly sickled cells (ISCs) remain sickled even under conditions where they are well oxygenated and hemoglobin is depolymerized. In our studies we demonstrate that triton extracted ISC core skeletons containing only spectrin, protein 4.1, and actin also retain their sickled shape; while reversibly sickled cell (RSC) skeletons remodel to a round or biconcave shape. We also demonstrate that these triton extracted ISC core skeletons dissociate more slowly upon incubation at 37 degrees C than do RSC or control (AA) core skeletons. This observation may supply the basis for the inability of the ISC core skeleton to remodel its shape. Using an in vitro ternary complex dissociation assay, we demonstrate that a modification in beta-actin is the major determinant of the slow dissociation of the spectrin-protein 4.1-actin complex isolated from the ISC core skeleton. We demonstrate that the difference between ISC and control beta-actin is the inaccessibility of two cysteine residues in ISC beta-actin to labeling by thiol reactive reagents; due to the formation of a disulfide bridge between cysteine284 and cysteine373 in ISC beta-actin, or alternatively another modification of cysteine284 and cysteine373 which is reversible with DTT and adds less than 100 D to the molecular weight of beta-actin. SN - 0021-9525 UR - https://www.unboundmedicine.com/medline/citation/7876306/A_posttranslational_modification_of_beta_actin_contributes_to_the_slow_dissociation_of_the_spectrin_protein_4_1_actin_complex_of_irreversibly_sickled_cells_ L2 - https://rupress.org/jcb/article-lookup/doi/10.1083/jcb.128.5.805 DB - PRIME DP - Unbound Medicine ER -