Interaction of nectin with afadin is necessary for its clustering at cell-cell contact sites but not for its cis dimerization or trans interaction
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Structural features of nectin-2 (HveB) required for herpes simplex virus entryNectin-2 is a potential target for antibody therapy of breast and ovarian cancersImplications of nectin-like molecule-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion and transmembrane protein localization in epithelial cellsCellular localization of nectin-1 and glycoprotein D during herpes simplex virus infectionMutations in the N-terminal domains of nectin-1 and nectin-2 reveal differences in requirements for entry of various alphaherpesviruses and for nectin-nectin interactions.ADIP, a novel Afadin- and alpha-actinin-binding protein localized at cell-cell adherens junctionsCell-to-cell spread of wild-type herpes simplex virus type 1, but not of syncytial strains, is mediated by the immunoglobulin-like receptors that mediate virion entry, nectin1 (PRR1/HveC/HIgR) and nectin2 (PRR2/HveB)Synaptopodin couples epithelial contractility to α-actinin-4-dependent junction maturationBiochemical and Structural Definition of the l-Afadin- and Actin-binding Sites of alpha -CateninCrystal Structure of the cis-Dimer of Nectin-1: IMPLICATIONS FOR THE ARCHITECTURE OF CELL-CELL JUNCTIONSNectin ectodomain structures reveal a canonical adhesive interfaceStructure of Nectin-2 reveals determinants of homophilic and heterophilic interactions that control cell-cell adhesionNectin-3, a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activitiesThe tumor suppressor protein TSLC1 is involved in cell-cell adhesionRecruitment of nectin-3 to cell-cell junctions through trans-heterophilic interaction with CD155, a vitronectin and poliovirus receptor that localizes to alpha(v)beta3 integrin-containing membrane microdomainsProminent role of the Ig-like V domain in trans-interactions of nectins. Nectin3 and nectin 4 bind to the predicted C-C'-C"-D beta-strands of the nectin1 V domainKRIT-1/CCM1 is a Rap1 effector that regulates endothelial cell cell junctionsTwo cell adhesion molecules, nectin and cadherin, interact through their cytoplasmic domain-associated proteinsNectin: an adhesion molecule involved in formation of synapsesNephrin and Neph1 co-localize at the podocyte foot process intercellular junction and form cis hetero-oligomersStriking similarity of murine nectin-1alpha to human nectin-1alpha (HveC) in sequence and activity as a glycoprotein D receptor for alphaherpesvirus entry.Tage4/Nectin-like molecule-5 heterophilically trans-interacts with cell adhesion molecule Nectin-3 and enhances cell migrationProliferative defects and formation of a double cortex in mice lacking Mltt4 and Cdh2 in the dorsal telencephalonA novel role of nectins in inhibition of the E-cadherin-induced activation of Rac and formation of cell-cell adherens junctions.GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Abeta42.Deletion of the second immunoglobulin-like domain of nectin-1 alters its intracellular processing and localization and ability to mediate entry of herpes simplex virusNectin-2 and N-cadherin interact through extracellular domains and induce apical accumulation of F-actin in apical constriction of Xenopus neural tube morphogenesis.Herpes simplex virus with highly reduced gD levels can efficiently enter and spread between human keratinocytes.Afadin controls cadherin cluster stability using clathrin-independent mechanism.Biological network inferences for a protection mechanism against familial Creutzfeldt-Jakob disease with E200K pathogenic mutation.Expression of the human poliovirus receptor/CD155 gene is activated by sonic hedgehog.Soluble V domain of Nectin-1/HveC enables entry of herpes simplex virus type 1 (HSV-1) into HSV-resistant cells by binding to viral glycoprotein DThe nectin-1alpha transmembrane domain, but not the cytoplasmic tail, influences cell fusion induced by HSV-1 glycoproteins.Amino acid substitutions in the V domain of nectin-1 (HveC) that impair entry activity for herpes simplex virus types 1 and 2 but not for Pseudorabies virus or bovine herpesvirus 1.Binding between the junctional proteins afadin and PLEKHA7 and implication in the formation of adherens junction in epithelial cells.Crystal structure of the V domain of human Nectin-like molecule-1/Syncam3/Tsll1/Igsf4b, a neural tissue-specific immunoglobulin-like cell-cell adhesion molecule.PLEKHA7 Recruits PDZD11 to Adherens Junctions to Stabilize NectinsEffects of herpes simplex virus on structure and function of nectin-1/HveC.The herpes simplex virus receptor nectin-1 is down-regulated after trans-interaction with glycoprotein D.Nectin proteins are expressed at early stages of nephrogenesis and play a role in renal epithelial cell morphogenesis.
P2860
Q24291800-CE87D221-C4E5-47E9-BC16-89062B7FCCB5Q24294932-0937D7A0-960D-4EB6-BDAC-EDBF2EB83C96Q24306339-DE005674-B670-43EE-9C1A-99E725BF744BQ24311876-5EF5AC50-68FD-4347-BFD9-01971F81A052Q24319105-3C88C205-04EA-4D4F-912A-A7F12DEA7DADQ24320219-41E0B8C6-D5EB-47F3-B74D-A615AEC2F7FDQ24524818-F6664991-0520-4E9B-8EA1-00ED0B5A1A23Q27310572-B45CE285-FC02-47E6-938E-CE9FF0AC48BCQ27638447-50F12516-A4FD-45E2-BA9A-9CF1BDE00EFEQ27666985-23875D92-01CF-4A18-86A5-327E3C058D02Q27671566-391DEC45-1026-47D0-AC4C-BE76F1A34AEBQ27671723-6E568539-DA96-406E-B021-3FB2DD0D52A8Q28140327-0BD0BA71-F111-4126-87C4-BA8E1D3DCACCQ28202664-0C5D9169-2FFA-4116-B541-6CACF705E73AQ28205394-98FC1409-278A-4ECA-BCC8-368A1633E32BQ28217548-7EF80727-0309-4DF6-BC7A-9C151274A875Q28254336-1938A4C6-FCDD-499B-B50B-15F2E3AB9CCCQ28511190-5F380702-9DDE-47DA-90ED-525BD301A758Q28577101-84A0FD67-61B1-40CF-8829-2E801687D1B6Q28577451-55E6DAE6-FF09-4F97-BDF9-FD35D5496C95Q28587515-747B7484-60B5-46BA-B125-44E5B2FDF9A1Q28587592-A7B990E2-8F63-46D8-AAB8-FD910F7738BFQ28592316-518CBB08-758C-4C71-AB50-6D691EB63F82Q30539011-80CBCD22-AA47-43EC-B2C8-DDFD96970738Q33276402-8CB41FD0-317C-491E-AAD2-7FB33A0AF6F7Q33737735-8EFE46D0-5B58-41A3-9EC0-4710F093F4D1Q33761248-CFBBFC7F-03EA-48EA-8F08-25BE91FED697Q33847925-91C0C9DB-D660-4594-9EFA-59F66A24D531Q33883289-1E5DDD77-05F1-4F7B-A3BB-E04FB117A39CQ34118329-AE449962-6184-40AA-AAC6-DA579C5A0F16Q34126107-2C0ABDBE-834F-46F2-A774-0368881F2288Q34233037-0960221C-CCB1-4124-A722-295F584E6870Q34333583-EEB6DEF1-170D-4B6D-9166-C174FCC9A665Q34342689-338683CD-2545-415E-A1AD-E8E05C8A3F3CQ34367505-77264E38-BFFF-4E99-9D2B-F740EE1B2847Q34492889-F2F722B7-BA12-431D-BB99-163E245E4602Q34520797-5F8CB415-AAEC-43CF-9688-1A70BACB97B5Q34970789-B3A3DACD-B119-4962-8537-FBF083BBE6ABQ37070391-743C29D1-44E5-45A1-B95A-2EDD602101FAQ37138803-46726461-4F90-4B26-933D-6CF1AD57F818
P2860
Interaction of nectin with afadin is necessary for its clustering at cell-cell contact sites but not for its cis dimerization or trans interaction
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Interaction of nectin with afa ...... erization or trans interaction
@ast
Interaction of nectin with afa ...... erization or trans interaction
@en
Interaction of nectin with afa ...... erization or trans interaction
@nl
type
label
Interaction of nectin with afa ...... erization or trans interaction
@ast
Interaction of nectin with afa ...... erization or trans interaction
@en
Interaction of nectin with afa ...... erization or trans interaction
@nl
prefLabel
Interaction of nectin with afa ...... erization or trans interaction
@ast
Interaction of nectin with afa ...... erization or trans interaction
@en
Interaction of nectin with afa ...... erization or trans interaction
@nl
P2093
P2860
P356
P1476
Interaction of nectin with afa ...... erization or trans interaction
@en
P2093
H Nakanishi
K Satoh-Horikawa
K Tachibana
K Takahashi
M Miyahara
P2860
P356
10.1074/JBC.275.1.613
P407
P577
2000-01-07T00:00:00Z