Interaction of membrane skeletal proteins with membrane lipid domain.

Sikorski, Aleksander F.; Hanus-Lorenz, Beata; Jezierski, Adam; Dluzewski, Anton R.

doi:10.18388/abp.2000_3979

Cited by 27 publications

(10 citation statements)

References 86 publications

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“…The organization of the plasma membrane in lipid domains affects its mechanical properties and the way it interacts with the underlying membrane skeleton (13). This interaction is believed to be critically important in the cochlear outer hair cell (OHC), one of the two types of sensory cells of the mammalian hearing organ.…”

Section: Introductionmentioning

confidence: 99%

Lateral Diffusion Anisotropy and Membrane Lipid/Skeleton Interaction in Outer Hair Cells

Monvel

Brownell

Ulfendahl

2006

Biophysical Journal

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The organization of the plasma membrane of cells in lipid domains affects the way the membrane interacts with the underlying protein skeleton, which in turn affects the lateral mobility of lipid and protein molecules in the membrane. Membrane fluidity properties can be monitored by various approaches, the most versatile of which is fluorescence recovery after photobleaching (FRAP). We extended previous FRAP experiments on isolated cochlear outer hair cells (OHCs) by analyzing the two-dimensional pattern of lipid diffusion in the lateral membrane of these cells. We found that membrane lipid mobility in freshly isolated OHCs is orthotropic, diffusion being faster in the axial direction of the cell and slower in the circumferential direction. Increasing the cell's turgor pressure by osmotic challenge reduced the axial diffusion constant, but had only a slight effect on circumferential diffusion. Our results suggest that lipid mobility in the OHC plasma membrane is affected by the presence of the cell's orthotropic membrane skeleton. This effect could reflect interaction with spectrin filaments or with other membrane skeletal proteins. We also performed a number of FRAP measurements in temporal bone preparations preserving the structural integrity of the hearing organ. The diffusion rates measured for OHCs in this preparation were in good agreement with those obtained in isolated OHCs, and comparable to the mobility rates measured on the sensory inner hair cells. These observations support the idea that the plasma membranes of both types of hair cells share similar highly fluid phases in the intact organ. Lipid mobility was significantly slower in the membranes of supporting cells of the organ of Corti, which could reflect differences in lipid phase or stronger hindrance by the cytoskeleton in these membranes.

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Section: Introductionmentioning

confidence: 99%

Lateral Diffusion Anisotropy and Membrane Lipid/Skeleton Interaction in Outer Hair Cells

Monvel

Brownell

Ulfendahl

2006

Biophysical Journal

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“…via spectrin's direct binding of phospholipids. There were many early indications that erythrocyte spectrin binds lipids in natural membranes (for a review see Sikorski et al, 2000;Grzybek et al, 2006). We found that non-erythroid spectrin (fodrin), similarly to erythroid spectrin, is able to bind aminophospholipids and also anionic phospholipids, with a reportedly even greater affinity Sikorski, 1995, 2002;Diakowski et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Lipid‐binding role of βII‐spectrin ankyrin‐binding domain

Bok

Plazuk

Hryniewicz-Jankowska

et al. 2007

Cell Biology International

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It is known that erythroid and non-erythroid spectrins binding of vesicles and monolayers containing PE proved sensitive to inhibition by red blood cell ankyrin. We now show that the bacterially-expressed recombinant peptides representing betaII(brain)-spectrin's ankyrin-binding domain and its truncated mutants showed lipid-binding activity, although only those containing a full-length amino terminal fragment showed high to moderate affinity towards phospholipid mono- and bilayers and a substantial sensitivity of this binding to inhibition by ankyrin. These results are in accordance with our published data on betaI-spectrin's ankyrin-binding domain [Hryniewicz-Jankowska A, et al. Mapping of ankyrin-sensitive, PE/PC mono- and bilayer binding site in erythroid beta-spectrin. Biochem J 2004;382:677-85]. Moreover, we tested also the effect of transient transfection of living cells of several cell-lines with vectors coding for GFP-conjugates including betaII and also betaI full-length ankyrin-binding domain and their truncated fragments on the membrane skeleton organization. The transfection with constructs encoding full-length ankyrin-binding domain of betaII and betaI spectrin resulted in increased aggregation of membrane skeleton and its punctate appearance in contrast to near normal appearance of membrane skeleton of cells transiently transfected with GFP control or construct encoding ankyrin-binding domain truncated at their N-terminal region. Our results therefore indicate the importance of N-terminal region for lipid-binding activity of the beta-spectrin ankyrin-binding domain and its substantial role in maintaining the spectrin-based skeleton distribution.

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“…The structure of this domain was recently resolved by Ipsaro et al (2009). In various experimental studies ZU5 has been shown to form a novel type of protein-protein interaction interface probably involved in binding of spectrins (Sikorski et al, 2000;Zhang et al, 2004). Here specifically, the co-localization near the cell membrane allows high affinity binding of ZU5 to signal transduction proteins (Ipsaro et al, 2009).…”

Section: Resultsmentioning

confidence: 99%

Unexpected domain composition of MACC1 links MET signaling and apoptosis.

Kokoszyńska

Kryński²,

Rychlewski³

et al. 2009

Acta Biochim Pol

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Colorectal cancer, one of the most challenging malignancies, still has a limited number of recognized prognostic and predictive markers indicating appropriate treatment. MACC1 (metastasis-associated in colon cancer-1), a novel regulator of tumor growth and metastasis has recently been identified as an important prognostic factor of metastatic disease in colorectal cancer. The mechanism of MACC1 activity remains undetermined. Here we apply a combination of fold recognition and homology modeling algorithms to draft MACC1 function. The applied methods revealed that the MACC1 protein consists of four domains: ZU5, SH3, and two C-terminal death domains (DD). Previously a similar domain architecture (ZU5-DD) was observed in other proteins, involved mainly in signal transduction and apoptosis regulation. Based on the specific aspects of the closest homologues' biology functional hypotheses on MACC1 are proposed. A broad range of bioinformatic analyzes indicates that MACC1, besides its involvement in signal transduction from the MET receptor, links MET signaling and apoptosis.

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Interaction of membrane skeletal proteins with membrane lipid domain.

Cited by 27 publications

References 86 publications

Lateral Diffusion Anisotropy and Membrane Lipid/Skeleton Interaction in Outer Hair Cells

Lateral Diffusion Anisotropy and Membrane Lipid/Skeleton Interaction in Outer Hair Cells

Lipid‐binding role of βII‐spectrin ankyrin‐binding domain

Unexpected domain composition of MACC1 links MET signaling and apoptosis.

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