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  VE-cadherin interacts with cell polarity protein Pals1 to regulate vascular lumen formation

Brinkmann, B. F., Steinbacher, T., Hartmann, C., Kummer, D., Pajonczyk, D., Mirzapourshafiyi, F., et al. (2016). VE-cadherin interacts with cell polarity protein Pals1 to regulate vascular lumen formation. MOLECULAR BIOLOGY OF THE CELL, 27(18), 2811-2821. doi:10.1091/mbc.E16-02-0127.

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Datensatz-Permalink: https://hdl.handle.net/21.11116/0000-0001-BD45-D Versions-Permalink: https://hdl.handle.net/21.11116/0000-0007-45BC-8
Genre: Zeitschriftenartikel

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 Urheber:
Brinkmann, Benjamin F., Autor
Steinbacher, Tim, Autor
Hartmann, Christian, Autor
Kummer, Daniel, Autor
Pajonczyk, Denise, Autor
Mirzapourshafiyi, Fatemeh1, Autor           
Nakayama, Masanori1, Autor           
Weide, Thomas, Autor
Gerke, Volker, Autor
Ebnet, Klaus, Autor
Affiliations:
1Cell Polarity and Organogenesis, Max Planck Institute for Heart and Lung Research, Max Planck Society, ou_2591702              

Inhalt

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Schlagwörter: 3-DIMENSIONAL COLLAGEN MATRIX; TIGHT-JUNCTION; ENDOTHELIAL-CELLS; SEGMENTAL DIFFERENTIATIONS; EPITHELIAL MORPHOGENESIS; CAPILLARY LUMEN; TUBE FORMATION; IN-VITRO; COMPLEX; MEMBRANECell Biology;
 Zusammenfassung: Blood vessel tubulogenesis requires the formation of stable cell-to-cell contacts and the establishment of apicobasal polarity of vascular endothelial cells. Cell polarity is regulated by highly conserved cell polarity protein complexes such as the Par3-aPKC-Par6 complex and the CRB3-Pals1-PATJ complex, which are expressed by many different cell types and regulate various aspects of cell polarity. Here we describe a functional interaction of VE-cadherin with the cell polarity protein Pals1. Pals1 directly interacts with VE-cadherin through a membrane-proximal motif in the cytoplasmic domain of VE-cadherin. VE-cadherin clusters Pals1 at cell-cell junctions. Mutating the Pals1-binding motif in VE-cadherin abrogates the ability of VE-cadherin to regulate apicobasal polarity and vascular lumen formation. In a similar way, deletion of the Par3-binding motif at the C-terminus of VE-cadherin impairs apicobasal polarity and vascular lumen formation. Our findings indicate that the biological activity of VE-cadherin in regulating endothelial polarity and vascular lumen formation is mediated through its interaction with the two cell polarity proteins Pals1 and Par3.

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Sprache(n): eng - English
 Datum: 2016
 Publikationsstatus: Erschienen
 Seiten: 11
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: ISI: 000384124700004
DOI: 10.1091/mbc.E16-02-0127
 Art des Abschluß: -

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Titel: MOLECULAR BIOLOGY OF THE CELL
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: 8120 WOODMONT AVE, STE 750, BETHESDA, MD 20814-2755 USA : AMER SOC CELL BIOLOGY
Seiten: - Band / Heft: 27 (18) Artikelnummer: - Start- / Endseite: 2811 - 2821 Identifikator: ISSN: 1059-1524