Ubiquitination of erythrocyte spectrin regulates the dissociation of the spectrin-adducin-f-actin ternary complex in vitro.
We demonstrate that ubiquitinated red blood cell (RBC) spectrin dissociates more rapidly from the spectrin-adducin-actin ternary complex, than non-ubiquitinated spectrin. Homozygous (SS) sickle cell spectrin has substantially diminished ubiquitination of alpha-spectrin resulting in slower dissociation from the spectrin-adducin-actin ternary complex, than normal (AA) cell spectrin. These results supply a partial explanation of the slow dissociation of the irreversible sickle cell (ISC) membrane skeleton, which leads to the inability of the ISC to change shape.
Mishra
R
R
Department of Molecular and Cell Biology, Sickle Cell Disease Research Center, Institute of Biomedical Sciences and Technology, University of Texas at Dallas, Richardson, TX, USA.
Goodman
S R
SR
D000199:Actins / Q000378:metabolism*; D000755:Anemia, Sickle Cell / Q000378:metabolism / Q000473:pathology; D002148:Calmodulin-Binding Proteins / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000378:metabolism; D006801:Humans; D046911:Macromolecular Substances; D011485:Protein Binding; D013049:Spectrin / Q000378:metabolism*; D025801:Ubiquitin / Q000378:metabolism*; D000099291:Adducins
D000199:Actins; D002148:Calmodulin-Binding Proteins; D046911:Macromolecular Substances; D013049:Spectrin; D025801:Ubiquitin; D000099291:Adducins