Concentration of an integral membrane protein, CD43 (leukosialin, sialophorin), in the cleavage furrow through the interaction of its cytoplasmic domain with actin-based cytoskeletons
about
Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domainRegulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositidesRedistribution of phosphatidylethanolamine at the cleavage furrow of dividing cells during cytokinesisRegulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathwayEzrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2ERM (ezrin/radixin/moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosisRho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail associationMoesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarizationLeukocyte ligands for endothelial selectins: specialized glycoconjugates that mediate rolling and signaling under flowStructural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex.Rho GTPase activity zones and transient contractile arraysNormal development of mice and unimpaired cell adhesion/cell motility/actin-based cytoskeleton without compensatory up-regulation of ezrin or radixin in moesin gene knockoutComparative proteomics reveals novel components at the plasma membrane of differentiated HepaRG cells and different distribution in hepatocyte- and biliary-like cellsThe terminal phase of cytokinesis in the Caenorhabditis elegans early embryo requires protein glycosylation.Assembly of cytoskeletal proteins into cleavage furrows of tissue culture cells.Identification of polymorphonuclear leukocyte and HL-60 cell receptors for adhesins of Streptococcus gordonii and Actinomyces naeslundii.Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor suppressor protein.CD43 interaction with ezrin-radixin-moesin (ERM) proteins regulates T-cell trafficking and CD43 phosphorylation.Disregulation of leukosialin (CD43, Ly48, sialophorin) expression in the B-cell lineage of transgenic mice increases splenic B-cell number and survival.Physiological contribution of CD44 as a ligand for E-Selectin during inflammatory T-cell recruitment.Cell adhesion and polarity during immune interactions.Formation of microvilli and phosphorylation of ERM family proteins by CD43, a potent inhibitor for cell adhesion: cell detachment is a potential cue for ERM phosphorylation and organization of cell morphology.Trafficking and recycling of the connexin43 gap junction protein during mitosis.Signaling through CD43 regulates CD4 T-cell traffickingAlbumin inhibits neutrophil spreading and hydrogen peroxide release by blocking the shedding of CD43 (sialophorin, leukosialin).Direct involvement of ezrin/radixin/moesin (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteins.A small, physiological electric field orients cell division.Glycosylation of CD44 negatively regulates its recognition of hyaluronan.ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons.Perturbation of cell adhesion and microvilli formation by antisense oligonucleotides to ERM family members.Protein kinase C theta (PKCtheta): a key player in T cell life and deathInhibition of cell adhesion by phosphorylated Ezrin/Radixin/Moesin.Three determinants in ezrin are responsible for cell extension activity.Aberrant glycosylation as biomarker for cancer: focus on CD43.Anti-tumor antibody BR96 blocks cell migration and binds to a lysosomal membrane glycoprotein on cell surface microspikes and ruffled membranesFly division.Truncation of monocyte chemoattractant protein 1 by plasmin promotes blood-brain barrier disruption.Chemokines regulate cellular polarization and adhesion receptor redistribution during lymphocyte interaction with endothelium and extracellular matrix. Involvement of cAMP signaling pathway.Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1
P2860
Q24313074-5C71BE4E-320F-4A74-9232-7BC386B86605Q24598762-F3D84768-30FC-49C4-BBDE-AF3E8E2E9235Q24645681-F7BE7740-37D7-4D6D-A414-9137D031F512Q24648177-D326E1E1-23A1-436D-9D8C-883A828265F2Q24671083-98DA2831-84C0-43EE-8EF9-A2430ADB33B8Q24676628-95F3DEAB-DA14-4BA9-8AB1-C3FA0AD61237Q24676652-2F4840D7-341F-462E-B7AF-80E707073462Q24678197-B7127A08-E9BE-4915-A50E-7C6E0CC6F3C3Q24683747-8CBEBEF1-0773-4E61-8879-ABB158DCC6DDQ27027232-C07238A8-4BBE-4B0F-93B0-4C808D67E9DCQ27640373-E980DDF4-619D-4969-BE57-4BCE8F55C4F3Q28265366-F144BDFD-A807-4337-8E66-54656A120DEBQ28508442-DB6EA10C-8DA5-4E4C-9C5D-3C323D255486Q28535470-1FBCEB2A-05E2-403E-9722-408FAD6C428DQ30476111-32AAC3AA-ECF5-4822-B471-7C6A1FA4191EQ33921479-8DA6B6C0-D1B0-4D35-8FB0-D136D2A4480DQ34005009-96026C51-6C27-4CEA-AFAF-F17FA42802D7Q34316029-265EB4C7-63E1-41AC-97A4-67AF79A270BAQ34749263-C641A7EB-4C0C-4847-9106-22C5ADDDA02FQ34786830-F780B022-E760-45BC-83C7-537D81338335Q34839368-4D079260-E9ED-4A72-93C8-632BC01997C3Q34862177-44443206-5CAF-406F-9724-B9E54994A944Q34891233-E752DBD6-9C8C-4ECC-8615-6140CB46EC32Q35738193-E0D03D5D-6677-4950-9A56-D045EEDE9332Q36059627-A1DBF6DF-A844-4805-8C3B-9AB4107A6966Q36232632-7DFE1E5C-275F-4A73-A575-6C9CF95393D2Q36256564-281805B4-9904-4F02-9B37-830ED3B4998DQ36333480-88B299BE-3B8C-4DB6-8545-3037DE48F358Q36365225-0E905FA1-608D-4B8C-A8D7-B3FC77C86316Q36382880-A78984E0-B856-4086-BD51-E074A3B1A33CQ36534860-CDF5F90F-C783-4759-B407-74364B642D7AQ36838094-0D85F554-7D8E-4BE8-B0BC-7253FA4E5A4DQ37114717-E07D50C2-6938-4B35-B591-41474715BDB9Q37387020-8D00D75B-9A60-4614-AADB-D78AE2CF02BFQ37618865-C2E8B2D9-19A0-4386-8562-515ED5472968Q38309858-54A7524C-ABE4-41C9-930C-BD06CCDE3B83Q40413972-33F8C048-0EFB-4E54-8065-E00710954029Q41825648-C1C8E4CB-8B7B-4508-85B9-0465DBD269FCQ41833771-8F5E6AC3-A3CD-4133-AB52-896CE080472FQ41834384-694350BF-A7F5-4DA8-BFB3-678023BC7E67
P2860
Concentration of an integral membrane protein, CD43 (leukosialin, sialophorin), in the cleavage furrow through the interaction of its cytoplasmic domain with actin-based cytoskeletons
description
1993 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի հունվարին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1993
@ast
im Januar 1993 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1993/01/01)
@sk
vědecký článek publikovaný v roce 1993
@cs
wetenschappelijk artikel (gepubliceerd op 1993/01/01)
@nl
наукова стаття, опублікована в січні 1993
@uk
مقالة علمية (نشرت عام 1993)
@ar
name
Concentration of an integral m ...... with actin-based cytoskeletons
@ast
Concentration of an integral m ...... with actin-based cytoskeletons
@en
Concentration of an integral m ...... with actin-based cytoskeletons
@nl
type
label
Concentration of an integral m ...... with actin-based cytoskeletons
@ast
Concentration of an integral m ...... with actin-based cytoskeletons
@en
Concentration of an integral m ...... with actin-based cytoskeletons
@nl
prefLabel
Concentration of an integral m ...... with actin-based cytoskeletons
@ast
Concentration of an integral m ...... with actin-based cytoskeletons
@en
Concentration of an integral m ...... with actin-based cytoskeletons
@nl
P2093
P2860
P356
P1476
Concentration of an integral m ...... with actin-based cytoskeletons
@en
P2093
A. Nagafuchi
S. Tsukita
S. Yonemura
P2860
P304
P356
10.1083/JCB.120.2.437
P407
P577
1993-01-01T00:00:00Z