ArticleThe Journal of cell biology1993
Concentration of an integral membrane protein, CD43 (leukosialin, sialophorin), in the cleavage furrow through the interaction of its cytoplasmic domain with actin-based cytoskeletons.
Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 146 citations in OpenAlex.
- Comprehensive in silico characterization of nonsynonymous SNPs in the human ezrin (EZR) gene and their role in disease pathogenesis.Biochemistry and biophysics reports · 2025Article
- Inhibition of cell adhesion by phosphorylated Ezrin/Radixin/Moesin.Cell adhesion & migration · 2015Article
- Aberrant glycosylation as biomarker for cancer: focus on CD43.BioMed research international · 2014Review
- Article
- Review
- Physiological contribution of CD44 as a ligand for E-Selectin during inflammatory T-cell recruitment.The American journal of pathology · 2011Article
- Truncation of monocyte chemoattractant protein 1 by plasmin promotes blood-brain barrier disruption.Journal of cell science · 2011Article
- CD43 interaction with ezrin-radixin-moesin (ERM) proteins regulates T-cell trafficking and CD43 phosphorylation.Molecular biology of the cell · 2011Article
- Trafficking and recycling of the connexin43 gap junction protein during mitosis.Traffic (Copenhagen, Denmark) · 2010Article
- Article
- Protein kinase C theta (PKCtheta): a key player in T cell life and death.Pharmacological research · 2007Review
- Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2007Article
- Rho GTPase activity zones and transient contractile arrays.BioEssays : news and reviews in molecular, cellular and developmental biology · 2006Review
- Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
- The terminal phase of cytokinesis in the Caenorhabditis elegans early embryo requires protein glycosylation.Molecular biology of the cell · 2005Article
- Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex.The EMBO journal · 2003Article
- Identification of polymorphonuclear leukocyte and HL-60 cell receptors for adhesins of Streptococcus gordonii and Actinomyces naeslundii.Infection and immunity · 2000Article
- Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain.The EMBO journal · 2000Article
- Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides.Molecular biology of the cell · 1999Article
- Direct involvement of ezrin/radixin/moesin (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteins.The Journal of cell biology · 1999Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In leukocytes such as thymocytes and basophilic leukemia cells, a glycosilated integral membrane protein called CD43 (leukosialin or sialophorin), which is defective in patients with Wiskott-Aldrich syndrome, was highly concentrated in the cleavage furrow during cytokinesis. Not only at the mitotic phase but also at interphase, CD43 was precisely colocalized with ezrin-radixin-moesin family members. (ERM), which were previously reported to play an important role in the plasma membrane-actin filament association in general. At the electron microscopic level, throughout the cell cycle, both CD43 and ERM were tightly associated with microvilli, providing membrane attachment sites for actin filaments. We constructed a cDNA encoding a chimeric molecule consisting of the extracellular domain of mouse E-cadherin and the transmembrane/cytoplasmic domain of rat CD43, and introduced it into mouse L fibroblasts lacking both endogenous CD43 and E-cadherin. In dividing transfectants, the chimeric molecules were concentrated in the cleavage furrow together with ERM, and both proteins were precisely colocalized throughout the cell cycle. Furthermore, using this transfection system, we narrowed down the domain responsible for the CD43-concentration in the cleavage furrow. Based on these findings, we conclude that CD43 is concentrated in the cleavage furrow through the direct or indirect interaction of its cytoplasmic domain with ERM and actin filaments.
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