Abstract:
:Defects or deficiencies in red cell membrane skeletal proteins often undermine the integrity and stability of the plasma membrane, and consequently cause hereditary hemolytic anemias. Genetic and biochemical studies have revealed a complicated picture of the organization of the membrane skeleton, within which α-/β-spectrin heterodimers form a protein lattice. By stabilizing the red cell membrane skeleton, the erythroid protein 4.1R greatly contributes to connecting and regulating the interaction among spectrins, actin filaments and integral proteins on the plasma membrane. In this study, we demonstrated the direct interaction between 4.1R and α-/β-spectrin. The results provide novel insights into the stoichiometry of 4.1R with spectrin, and demonstrate for the first time that the binding ratio of 4.1R to spectrin heterodimers is approximately 5.
journal_name
Mol Med Repjournal_title
Molecular medicine reportsauthors
Zhang DQ,Wang YP,Wang WH,Sui XM,Jiang JQ,Jiang XM,Xu ZS,Liu YGdoi
10.3892/mmr.2011.470subject
Has Abstractpub_date
2011-07-01 00:00:00pages
651-4issue
4eissn
1791-2997issn
1791-3004journal_volume
4pub_type
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