Involvement of LMO7 in the association of two cell-cell adhesion molecules, nectin and E-cadherin, through afadin and alpha-actinin in epithelial cells
about
Insights into the molecular evolution of the PDZ/LIM family and identification of a novel conserved protein motifThe diversification of the LIM superclass at the base of the metazoa increased subcellular complexity and promoted multicellular specializationThe nuclear envelope LEM-domain protein emerinSynaptopodin couples epithelial contractility to α-actinin-4-dependent junction maturationAlp/Enigma family proteins cooperate in Z-disc formation and myofibril assemblyConcomitant binding of Afadin to LGN and F-actin directs planar spindle orientationIntestinal barrier function: molecular regulation and disease pathogenesisMicroRNA-23b regulates cellular architecture and impairs motogenic and invasive phenotypes during cancer progressionZasp52, a Core Z-disc Protein in Drosophila Indirect Flight Muscles, Interacts with α-Actinin via an Extended PDZ DomainRegulation of cadherin-mediated adhesion in morphogenesismiR-23b regulates cytoskeletal remodeling, motility and metastasis by directly targeting multiple transcriptsPDLIM1 inhibits NF-κB-mediated inflammatory signaling by sequestering the p65 subunit of NF-κB in the cytoplasm.A Marfan syndrome gene expression phenotype in cultured skin fibroblasts.Identification of a putative network of actin-associated cytoskeletal proteins in glomerular podocytes defined by co-purified mRNAsLIMCH1 regulates nonmuscle myosin-II activity and suppresses cell migration.Afadin controls cadherin cluster stability using clathrin-independent mechanism.RNA-binding protein RBM20 represses splicing to orchestrate cardiac pre-mRNA processing.Anchoring junctions as drug targets: role in contraceptive development.Lmo7 is an emerin-binding protein that regulates the transcription of emerin and many other muscle-relevant genes.LMO7 mediates cell-specific activation of the Rho-myocardin-related transcription factor-serum response factor pathway and plays an important role in breast cancer cell migration.Cholesterol depletion induces transcriptional changes during skeletal muscle differentiation.Emerin in health and disease.Loss of AF-6/afadin induces cell invasion, suppresses the formation of glandular structures and might be a predictive marker of resistance to chemotherapy in endometrial cancerRoles of nectins in cell adhesion, migration and polarization.Lmo7 is dispensable for skeletal muscle and cardiac function.Decreased expression of LMO7 and its clinicopathological significance in human lung adenocarcinoma.High CO2 Leads to Na,K-ATPase Endocytosis via c-Jun Amino-Terminal Kinase-Induced LMO7b Phosphorylation.Vinculin-dependent Cadherin mechanosensing regulates efficient epithelial barrier formation.The N and C termini of ZO-1 are surrounded by distinct proteins and functional protein networks.Organization of multiprotein complexes at cell-cell junctions.Cell adhesion, the backbone of the synapse: "vertebrate" and "invertebrate" perspectives.Genes involved in type 1 diabetes: an updateNucleocytoplasmic functions of the PDZ-LIM protein family: new insights into organ development.Diseases of the Nucleoskeleton.Overview of the Muscle Cytoskeleton.Identification of genetic disparity between primary and metastatic melanoma in human patients.Knockdown of Lmo7 inhibits chick myogenesis.Regulation of the assembly and adhesion activity of E-cadherin by nectin and afadin for the formation of adherens junctions in Madin-Darby canine kidney cells.Involvement of the annexin II-S100A10 complex in the formation of E-cadherin-based adherens junctions in Madin-Darby canine kidney cells.Requirement of the actin cytoskeleton for the association of nectins with other cell adhesion molecules at adherens and tight junctions in MDCK cells.
P2860
Q21144465-542EECEA-1EA6-41B0-BF99-7BF962F5CB84Q21560967-28E78FB0-E884-4733-AB17-A43766610D75Q26826857-C6CD279E-4217-41AF-9710-253CF82F918BQ27310572-2BBCE5AF-2137-48D5-AFED-A1C65EFB0FD6Q27324201-345EEE8B-5404-4CBB-9539-B87B85FA8FBEQ27703589-EE4F5B8A-3F2C-4CEA-9B8A-6A9E6954C353Q28250081-6AAB039E-E1F3-4465-941A-4A345CECEF69Q28297863-354B2714-13F5-442B-BAC6-E8B0EFF90C45Q28552972-7953F945-06CA-4ADF-BAAE-B1C058681233Q29614940-98E26D20-0196-4680-8C15-0B4B223BEC49Q30540092-01F8AD6A-2C29-4C64-B31B-01A13A49EF07Q31032656-5F4E49E6-B110-4FAD-AC8B-5C2EB7EB2DDEQ33298689-8A218505-B7C6-4B38-8F64-38A13BDFBCC4Q33490128-37A9B541-CB02-4215-8044-D592E629D2E7Q33563355-FAFE79E1-B87E-4AEB-9B94-18F6FD9C78DDQ33883289-51D3D523-6499-487A-90A2-8F141E53EF85Q33944218-44910145-6FB2-4DCB-8552-6A276816BE5FQ34501400-C7E18EEF-FBC0-4217-86BA-37D64FFB77FEQ34577033-FEFABCE5-E686-4E89-8D2A-7DBA7F6EA342Q35139962-65F19CEE-984D-4E9C-98D9-DBE3AD66F400Q35198692-3F0C2FA8-147E-4421-880A-FEBCA4E67667Q35259539-92CDC0F8-0DDB-479A-B595-7573B2267AF0Q35440276-EF150D0D-FD7D-41C2-9BCC-7F87874E2449Q35954748-FB9C98F1-2E52-42E9-8803-A1BA2FBB032DQ36122610-371877A4-1195-4148-88DE-9A6502C17DC1Q36230875-9F50EA48-C661-45BD-AC9A-9450DBB9AB59Q36234268-D99C065C-F575-4E6F-9B1D-60B94D2E49B7Q36425571-EA4C2DE9-A846-48BA-B5F7-626BB4F2C3EEQ36832696-E8182F51-2F57-4AB2-B56C-279DAAE12BA7Q37118549-EC528934-744D-4CEF-A33B-AC7D8D8E64FCQ37412638-33F2EFCA-D4F8-4794-8513-E1BEFD6B3970Q37585015-3D8284D5-58F4-45DD-B8CC-1F344ADB110BQ37679075-7FEF57B9-7A23-4DE4-A6CF-EAAD152E4F0CQ38991463-1CA6AD16-3271-40C7-9BEF-A0BEA9A2C242Q39391006-DC1E9519-68C3-4E37-B763-C3F59C2461EFQ39541129-6F9A09AD-7467-401A-9431-D21B5E258D00Q40087704-19155BF8-1DD0-467E-98D5-A52DA0413FE2Q40338912-73F869E8-4A0D-4B6E-BA8B-AA75F6D97EF1Q40485882-2B80490E-BDE4-4F7F-A2DF-A44E45B4B83DQ40522184-B91870F4-FCFD-4F3B-AD34-378B8E9EF503
P2860
Involvement of LMO7 in the association of two cell-cell adhesion molecules, nectin and E-cadherin, through afadin and alpha-actinin in epithelial cells
description
2004 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2004
@ast
im Juli 2004 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2004/07/23)
@sk
vědecký článek publikovaný v roce 2004
@cs
wetenschappelijk artikel (gepubliceerd op 2004/07/23)
@nl
наукова стаття, опублікована в липні 2004
@uk
name
Involvement of LMO7 in the ass ...... ha-actinin in epithelial cells
@ast
Involvement of LMO7 in the ass ...... ha-actinin in epithelial cells
@en
Involvement of LMO7 in the ass ...... ha-actinin in epithelial cells
@nl
type
label
Involvement of LMO7 in the ass ...... ha-actinin in epithelial cells
@ast
Involvement of LMO7 in the ass ...... ha-actinin in epithelial cells
@en
Involvement of LMO7 in the ass ...... ha-actinin in epithelial cells
@nl
prefLabel
Involvement of LMO7 in the ass ...... ha-actinin in epithelial cells
@ast
Involvement of LMO7 in the ass ...... ha-actinin in epithelial cells
@en
Involvement of LMO7 in the ass ...... ha-actinin in epithelial cells
@nl
P2093
P2860
P3181
P356
P1476
Involvement of LMO7 in the ass ...... ha-actinin in epithelial cells
@en
P2093
Kenji Irie
Koji Morimoto
Takako Ooshio
Toshio Imai
Yoshimi Takai
P2860
P304
31365-31373
P3181
P356
10.1074/JBC.M401957200
P407
P577
2004-05-12T00:00:00Z