The red cell membrane and its cytoskeleton

Gratzer, Walter

doi:10.1042/bj1980001

Cited by 126 publications

(56 citation statements)

References 71 publications

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“…First, the PI(4,5)P 2 concentration in the PM has been determined using erythrocytes (11,20,28). These cells have a unique cytoskeleton structure (5,27,86) and lack the regular endocytosis function (77). As actin cytoskeleton rearrangement and endocytosis are two major PI(4,5)P 2 -regulated cellular functions in other cell types (13,47,49,85), PI(4,5)P 2 levels in erythrocytes may differ from those in other cell types.…”

Section: Discussionmentioning

confidence: 99%

Interaction between the Human Immunodeficiency Virus Type 1 Gag Matrix Domain and Phosphatidylinositol-(4,5)-Bisphosphate Is Essential for Efficient Gag Membrane Binding

Chukkapalli

Hogue

Boyko

et al. 2008

J Virol

243

386

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Human immunodeficiency virus type 1 (HIV-1) particle assembly mediated by the viral structural protein Gag occurs predominantly on the plasma membrane (PM). Although it is known that the matrix (MA) domain of Gag plays a major role in PM localization, molecular mechanisms that determine the location of assembly remain to be elucidated. We observed previously that overexpression of polyphosphoinositide 5-phosphatase IV (5ptaseIV) that depletes PM phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P 2 ] impairs virus particle production and redirects processed Gag to intracellular compartments. In this study, we examined the impact of PI(4,5)P 2 depletion on the subcellular localization of the entire Gag population using Gag-fluorescent protein chimeras. Upon 5ptaseIV overexpression, in addition to perinuclear localization, Gag also showed a hazy cytosolic signal, suggesting that PI(4,5)P 2 depletion impairs Gag membrane binding. Indeed, Gag was less membrane bound in PI(4,5)P 2 -depleted cells, as assessed by biochemical analysis. These observations are consistent with the hypothesis that Gag interacts with PI(4,5)P 2 . To examine a putative Gag interaction with PI(4,5)P 2 , we developed an in vitro binding assay using full-length myristoylated Gag and liposome-associated PI(4,5)P 2 . Using this assay, we observed that PI(4,5)P 2 significantly enhances liposome binding of wild-type Gag. In contrast, a Gag derivative lacking MA did not require PI(4,5)P 2 for efficient liposome binding. To analyze the involvement of MA in PI(4,5)P 2 binding further, we examined MA basic amino acid substitution mutants. These mutants, previously shown to localize in perinuclear compartments, bound PI(4,5)P 2 -containing liposomes weakly. Altogether, these results indicate that HIV-1 Gag binds PI(4,5)P 2 on the membrane and that the MA basic domain mediates this interaction.

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Section: Discussionmentioning

confidence: 99%

Interaction between the Human Immunodeficiency Virus Type 1 Gag Matrix Domain and Phosphatidylinositol-(4,5)-Bisphosphate Is Essential for Efficient Gag Membrane Binding

Chukkapalli

Hogue

Boyko

et al. 2008

J Virol

243

386

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“…There is good evidence that in these cells a network of peripheral mem brane protein, called spectrin (probably in conjunction with an actin-like protein), con trols the mobility and topography of integral membrane proteins [8], Spectrin is exclu sively located on the cytoplasmic (i.e. inner) surface of erythrocyte membranes, presum ably bound to negatively charged phospho lipids [9], The spectrin network may be im portant in the resistance to cell deformation and in maintaining the biconcave shape of the cell [10].…”

mentioning

confidence: 99%

“…Chemical probes also provide informa tion about the localization of membrane pro- teins and this, combined with data from en zymatic labelling in a similar experimental set-up, has led to an almost complete topo graphical picture of the human erythrocyte membrane [8,20] (fig. II).…”

mentioning

confidence: 99%

Blood Cell Membranes and Haemostasis

Zwaal¹,

Hemker²

1982

Pathophysiol Haemos Thromb

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“…The proteins of human erythrocyte membrane have been extensively studied with respect to their structure and organization in last three decades (Gratzer 1981;Kakhniashvili et al 2004). Over 250 blood group determinants are known and most of these are located on integral erythrocyte proteins and glycoproteins.…”

Section: Discussionmentioning

confidence: 99%

Differential actions of proteinases and neuraminidase on mammalian erythrocyte surface and its impact on erythrocyte agglutination by concanavalin A

Sharma

Gokhale²

2012

gpb

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Abstract. Action of proteinases viz. trypsin and chymotrypsin, and neuraminidase on intact erythrocyte membrane proteins and glycophorins (sialoglycoproteins) exposed to cell surface and its impact on lectin (concanavalin A)-mediated agglutination were studied in Homo sapiens (human), Capra aegagrus hircus (goat) and Bubalus bubalis (buffalo). Membrane proteins and glycophorins analysis by SDS-PAGE as visualized by coomassie brilliant blue and periodic acid-schiff stains, respectively, and agglutination behaviour revealed marked differences: 1) there were prominent dissimilarities in the number and molecular weights of glycophorins in human, goat and buffalo erythrocyte membranes; 2) proteinase action(s) on human and buffalo erythrocyte surface membrane proteins and glycophorins showed similarity but was found different in goat; 3) significant differences in erythrocyte agglutinability with concanavalin A can be attributed to differences in membrane composition and alterations in the surface proteins after enzyme treatment; 4) a direct correlation was found between degradation of glycophorins and concanavalin A agglutinability; 5) action of neuraminidase specifically indicated the negative role of cell surface sialic acids in determining concanavalin A agglutinability of goat and buffalo erythrocytes, similar to human. Present studies clearly indicate that there are some basic differences in human, goat and buffalo erythrocyte membrane proteins, especially with respect to glycophorins, which determine the concanavalin A-mediated agglutination in enzyme treated erythrocytes.

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The red cell membrane and its cytoskeleton

Cited by 126 publications

References 71 publications

Interaction between the Human Immunodeficiency Virus Type 1 Gag Matrix Domain and Phosphatidylinositol-(4,5)-Bisphosphate Is Essential for Efficient Gag Membrane Binding

Interaction between the Human Immunodeficiency Virus Type 1 Gag Matrix Domain and Phosphatidylinositol-(4,5)-Bisphosphate Is Essential for Efficient Gag Membrane Binding

Blood Cell Membranes and Haemostasis

Differential actions of proteinases and neuraminidase on mammalian erythrocyte surface and its impact on erythrocyte agglutination by concanavalin A

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The red cell membrane and its cytoskeleton

Cited by 126 publications

References 71 publications

Interaction between the Human Immunodeficiency Virus Type 1 Gag Matrix Domain and Phosphatidylinositol-(4,5)-Bisphosphate Is Essential for Efficient Gag Membrane Binding

Interaction between the Human Immunodeficiency Virus Type 1 Gag Matrix Domain and Phosphatidylinositol-(4,5)-Bisphosphate Is Essential for Efficient Gag Membrane Binding

Blood Cell Membranes and Haemostasis

Differential actions of proteinases and neuraminidase on mammalian erythrocyte surface and its impact on erythrocyte agglutination by concanavalin A

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Resources

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Differential actions of proteinases and neuraminidase on mammalian erythrocyte surface and its impact on erythrocyte agglutination by concanavalin A