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7 Cellular and Molecular Biology Letters

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Crystal structure F-actin binding domain from human beta-spectrin

100%

Djinovic Carugo K. , Banuelos S. , Saraste M.

Cellular and Molecular Biology Letters

1998

tom 03

nr 2

Molecular studies of the erythrocyte spectrin tetramerization region

88%

Park S. , Mehboob S. , Luo B. H. , Hurtuk M. G. , Johnson M. E. , Fung L. W. M.

Cellular and Molecular Biology Letters

2001

tom 06

nr 2

BetaII spectrins and fodaxins: interacting proteins in many tissues

75%

Baines A. J. , Ohanian V. , Heerkens E. , Phillips G. , Hayes N. V. L.

Cellular and Molecular Biology Letters

1998

tom 03

nr 2

The effect of the lipid-binding site of the ankyrin-binding domain of erythroid beta-spectrin on the properties of natural membranes and skeletal structures

63%

Chorzalska A. , Lach A. , Borowik T. , Wolny M. , Hryniewicz-Jankowska A. , Kolondra A. , Langner M. , Sikorski A. F.

tom 15

nr 3

406-423

It was previously shown that the beta-spectrin ankyrin-binding domain binds lipid domains rich in PE in an ankyrin-dependent manner, and that its N-terminal sequence is crucial in interactions with phospholipids. In this study, the effect of the full-length ankyrin-binding domain of β-spectrin on natural erythrocyte and HeLa cell membranes was tested. It was found that, when encapsulated in resealed erythrocyte ghosts, the protein representing the full-length ankyrin-binding domain strongly affected the shape and barrier properties of the erythrocyte membrane, and induced partial spectrin release from the membrane, while truncated mutants had no effect. As found previously (Bok et al. Cell Biol. Int. 31 (2007) 1482–94), overexpression of the full-length GFP-tagged ankyrin-binding domain aggregated and induced aggregation of endogenous spectrin, but this was not the case with overexpression of proteins truncated at their N-terminus. Here, we show that the aggregation of spectrin was accompanied by the aggregation of integral membrane proteins that are known to be connected to spectrin via ankyrin, i.e. Na+K+ATP-ase, IP3 receptor protein and L1 CAM. By contrast, the morphology of the actin cytoskeleton remained unchanged and aggregation of cadherin E or N did not occur upon the overexpression of either full-length or truncated ankyrin-binding domain proteins. The obtained results indicate a substantial role of the lipid-binding part of the β-spectrin ankyrin-binding domain in the determination of the membrane and spectrin-based skeleton functional properties.

Isoforms distribution and activities of beta spectrins and 4.1 proteins in brain

63%

Baines A. J. , Bignone P. A. , Hayes N. V. L. , Keating L. A. , Phillips G. W. , Scott C.

Cellular and Molecular Biology Letters

2001

tom 06

nr 2

Spectrin isoform diversity and assembly in non-erythroid cells

51%

Cianci C. D. , Kim J. C. , McLaughlin J. , Stabach P. R. , Lombardo C. R. , Morrow J. S.

Cellular and Molecular Biology Letters

1996

tom 01

nr 1

Four human spectrin genes are now recognized. Two encode alpha spectrins (αI and αII), the other two encode beta spectrins (βI and βII). Multiple alternatively spliced transcripts have also been identified for all but al spectrin, yielding a subtle but rich diversity of possible ap spectrin heterodimer species in most cells. The role of these isoforms and the factors that control their assembly into the triton-insoluble cortical membrane skeleton are poorly understood. RT-PCR analysis using primers flanking regions of alternative mRNA spicing for αII, βI, and βII spectrin have been used to explore the diversity of isoform expression in cultured fibroblasts, MDCK cells, and PC12 cells. Factors that stimulate assembly or redistribution of the spectrin skeleton in these cells were also sought. Several isoforms of spectrin are expressed in each of these cell lines, and PC12 cells altered the balance of one isoform moderately in response to NGF stimulation. These three cell lines also illustrate different ways that the assembly of the cortical skeleton may be regulated. In SV40tsA58 temperature sensitive large T transformed fibroblasts, spectrin redistributes from a largely cytoplasmic distribution to focal membrane patches upon transformation; in MDCK cells, cell-cell contact initiates spectrin assembly; in PC12 cells, stimulation with growth factor (NGF) induces a redistribution of spectrin from membrane to cytoplasmic pools. Collectively, these results suggest that both cell-cell contact and growth factor mediated signaling mechanisms control the assembly and isoform composition of the spectrin cytoskeleton, and highlight the complexity of this process.

The lamprey [Lampetra fluviatilis] erythrocyte; morphology, ultrastructure, major plasma membrane proteins and phospholipids, and cytoskeletal organization

51%

Hagerstrand H. , Danieluk M. , Nikinmaa M.

Cellular and Molecular Biology Letters

1998

tom 03

nr 2