A protein immunologically related to erythrocyte band 4.1 is found on stress fibres of non-erythroid cells

Cohen, Carl M.; Foley, Susan F.; Korsgren, Catherine

doi:10.1038/299648a0

Cited by 140 publications

(59 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…4.1R deficiency in platelets of the knockout mouse was confirmed by immunoblot experiments, which revealed a weak expression of an ∼75-kDa immunoreactive band in normal platelets (35,36) . Platelet morphology, examined either in Wrightstained blood smears (data not shown) or in transmission electron micrographs of buffy coat fractions (Fig.…”

mentioning

confidence: 80%

Protein 4.1R–deficient mice are viable but have erythroid membrane skeleton abnormalities

et al. 1999

View full text Add to dashboard Cite

A diverse family of protein 4.1R isoforms is encoded by a complex gene on human chromosome 1. Although the prototypical 80-kDa 4.1R in mature erythrocytes is a key component of the erythroid membrane skeleton that regulates erythrocyte morphology and mechanical stability, little is known about 4.1R function in nucleated cells. Using gene knockout technology, we have generated mice with complete deficiency of all 4.1R protein isoforms. These 4.1R-null mice were viable, with moderate hemolytic anemia but no gross abnormalities. Erythrocytes from these mice exhibited abnormal morphology, lowered membrane stability, and reduced expression of other skeletal proteins including spectrin and ankyrin, suggesting that loss of 4.1R compromises membrane skeleton assembly in erythroid progenitors. Platelet morphology and function were essentially normal, indicating that 4.1R deficiency may have less impact on other hematopoietic lineages. Nonerythroid 4.1R expression patterns, viewed using histochemical staining for lacZ reporter activity incorporated into the targeted gene, revealed focal expression in specific neurons in the brain and in select cells of other major organs, challenging the view that 4.1R expression is widespread among nonerythroid cells. The 4.1R knockout mice represent a valuable animal model for exploring 4.1R function in nonerythroid cells and for determining pathophysiological sequelae to 4.1R deficiency.

show abstract

mentioning

confidence: 80%

Protein 4.1R–deficient mice are viable but have erythroid membrane skeleton abnormalities

et al. 1999

View full text Add to dashboard Cite

show abstract

“…In the erythrocyte, ankyrin and protein 4.1 mediate the attachment of the spectrin-actin cortical cytoskeleton to the integral membrane proteins band 3 and glycophorin (for reviews, Bennett, 1985;Morrow and Anderson, 1986). Analogues of ankyrin, protein 4.1, and band 3 also enjoy a wide tissue distribution (e.g., see Bennett, 1985;Spiegel et al, 1984;Cohen et al, 1982;Granger and Lazarides, 1985;Drenckhahn et al, 1984). Much less is known about the ability of ankyrin to mediate the attachment of the spectrin-actin skeleton to other integral membrane proteins unrelated to band 3.…”

mentioning

confidence: 99%

Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells.

Morrow

Cianci

Ardito

et al. 1989

The Journal of Cell Biology

263

113

View full text Add to dashboard Cite

Abstract. In nonerythroid cells the distribution of the cortical membrane skeleton composed of fodrin (spectrin), actin, and other proteins varies both temporally with cell development and spatially within the cell and on the membrane. In monolayers of Madin-Darby canine kidney (MDCK) cells, it has previously been shown that fodrin and Na,K-ATPase are codistributed asymmetrically at the basolateral margins of the cell, and that the distribution of fodrin appears to be regulated posttranslationally when confluence is achieved (Nelson, W. J., and P. I. Veshnock. 1987. J. Cell Biol. 104:1527-1537. The molecular mechanisms underlying these changes are poorly understood. We find that (a) in confluent MDCK cells and intact kidney proximal tubule cells, Na,K-ATPase, fodrin, and analogues of human erythrocyte ankyrin are precisely colocalized in the basolateral domain at the ultrastructural level. (b) This colocalization is only achieved in MDCK cells after confluence is attained. (c) Erythrocyte ankyrin binds saturably to Na,K-ATPase in a molar ratio of ",d ankyrin to 4 Na,K-ATPase's, with a kD of 2.6/~M. (d) The binding of ankyrin to Na,K-ATPase is inhibited by the 43-kD cytoplasmic domain of erythrocyte band 3. (e) ~25I-labeled ankyrin binds to the alpha subunit of Na,K-ATPase in vitro. There also appears to be a second minor membrane protein of • 240 kD that is associated with both erythrocyte and kidney membranes that binds ~25I-labeled ankyrin avidly. The precise identity of this component is unknown. These results identify a molecular mechanism in the renal epithelial cell that may account for the polarized distribution of the fodrin-based cortical cytoskeleton.

show abstract

“…Our immunoprecipitation experiments using a specific erythrocyte 4.1 antibody followed by SDS PAGE and autoradiographic analysis reveals that the lymphoma 4.l-like protein consists of a doublet of 68,000 and 65,000 D. It is not surprising to find a 4.l-like protein in lymphocytes that differs in molecular mass from the erythrocyte band 4.1. Molecular mass variants have been observed in a number of different cell types of both erythroid and non-erythroid origin (5,23,33,34,62). These variations clearly do not necessarily reflect differences in 4.1 function since all of the different molecular mass forms still retain their ability to bind spectrin or fodrin (6).…”

Section: Discussionmentioning

confidence: 99%

“…Nonerythroid 4.l-like proteins (ranging in molecular mass from 68,000 to 80,000 D) have been identified in several different cell types (5,23,33,34,62). It has been demonstrated that at least one of these non-erythroid 4.l-like molecules can be phosphorylated by a cAMP-dependent kinase (6,38,50,60).…”

Section: Identification Of the 68/65-kd Doublet As A 4l-like Proteinmentioning

confidence: 99%

“…Recently, immunoreactive forms of band 4.1 have been identified in brain tissue (6,33), in fibroblasts (23), and in several blood cell types such as lymphocytes, platelets, and polymorphonuclear leukocytes (62). In these nonerythroid cells, the immunoreactive 4.1 proteins appear as either a singlet or a doublet with apparent molecular masses ranging from 68,000 to 75,000 D after SDS PAGE (8).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Lymphoma Thy-1 glycoprotein is linked to the cytoskeleton via a 4.1-like protein.

Bourguignon¹,

Suchard²,

Kalomiris³

1986

The Journal of Cell Biology

View full text Add to dashboard Cite

Abstract. In this study we have found that the phosphoprotein doublet of 68,000 and 65,000 daltons (68/65 kD) in mouse T-lymphoma cells shares several structural and functional similarities with erythrocyte band 4.1. Our evidence for identifying the 68/65-kD doublet as a lymphoma 4.l-like protein is as follows: (a) it displays an immunological cross-reactivity with anti-erythrocyte band 4.1 antibody; (b) it exhibits a Svedberg unit of sedimentation coefficient of 4 S; (c) it is phosphorylated in the presence of phorbol ester (phorbol-12-O-tetradecanoylphorbol-B-acetate) and its phosphorylation requires Ca2+; (d) it is phosphorylater primarily at serine residues; and (e) it can bind directly to fodrin (a spectrin-like actin-binding protein). In addition, this lymphoma 4.l-like protein can be both colocalized and coisolated with the major T-lymphocyte-specific glycoprotein, Thy-1 (gp 25). Therefore, all of these results strongly suggest that the lymphoma 4.l-like protein (68/65-kD doublet) may play a pivotal role in linking the Thy-1 (gp 25) glycoprotein to fodrin which, in turn, binds to the actin filaments that are responsible for recruiting Thy-1 antigens into cap structures.

show abstract

A protein immunologically related to erythrocyte band 4.1 is found on stress fibres of non-erythroid cells

Cited by 140 publications

References 25 publications

Protein 4.1R–deficient mice are viable but have erythroid membrane skeleton abnormalities

Protein 4.1R–deficient mice are viable but have erythroid membrane skeleton abnormalities

Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells.

Lymphoma Thy-1 glycoprotein is linked to the cytoskeleton via a 4.1-like protein.

Contact Info

Product

Resources

About