Protein 4.1 deficiency associated with an altered binding to the spectrin-actin complex of the red cell membrane skeleton.

Abstract

Invest. 1994Invest. . 94:1651Invest. -1656

Spi-1/PU.1 but not Fli-1 inhibits erythroid-specific alternative splicing of 4.1R pre-mRNA in murine erythroleukemia cells

“…Indeed, it has been shown that 4.1R deficiency or the only defect of the 10 kDa SAB domain affects the stability of the spectrin-actin junctional complex Marchesi et al, 1990;Lorenzo et al, 1994;Maillet et al, 1999).…”

The Prototypical 4.1R-10-kDa Domain and the 4.1G-10-kDa Paralog Mediate Fodrin-Actin Complex Formation

“…Furthermore, a case of heterozygous hereditary elliptocytosis associated with partial deficiency of 4.1R has been reported in nine related French families (45). Molecular genetic analysis…”

Defining of the Minimal Domain of Protein 4.1 Involved in Spectrin-Actin Binding

“…Hence, a weak binary interaction with F-actin involving this motif might initiate ternary complex formation in vitro, even in the absence of high affinity spectrin binding. The importance of this putative actin motif is supported by 1) the fact that the shorter peptides 21.20 and 21.10, lacking part of the putative actin binding motif, displayed no activity in any of the assays, and 2) the recent observation that a protein 4.1 variant with a deletion of one residue from the Lys [447][448] doublet (corresponding to residues 20 -21 of this actin binding motif) is unable to interact with spectrin or spectrin-actin mixtures (49). Consistent with this model, a cooperative actin binding activity with protein 4.1 has been reported earlier using cosedimentation assays (6).…”