PuSH - Publikationsserver des Helmholtz Zentrums München

Export: TXT Text RIS Endnote (RIS) BIB BibTeX
Löer, B.* ; Bauer, R.* ; Bornheim, R.* ; Grell, J.* ; Kremmer, E. ; Kolanus, W.* ; Hoch, M.*

The NHL-domain protein Wech is crucial for the integrin-cytoskeleton link.

Nat. Cell Biol. 10, 422-428 (2008)
DOI
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
Integrin transmembrane receptors mediate cell adhesion through intracellular linker proteins that connect to the cytoskeleton. Of the numerous linker proteins identified, only a few, including Talin and Integrin-linked-kinase (ILK), are essential and evolutionarily conserved. The wech gene encodes a newly discovered and highly conserved regulator of integrin-mediated adhesion in Drosophila melanogaster. Embryos deficient in wech have very similar phenotypes to integrin-null or Talin-null embryos, including muscle detachment from the body wall. The Wech protein contains a B-box zinc-finger and a coiled-coil domain, which is also found in RBCC/TRIM family members, and an NHL domain. In beta-integrin or Talin mutants, Wech is mislocalized, whereas ILK localization depends on Wech. We provide evidence that Wech interacts with the head domain of Talin and the kinase domain of ILK, and propose that Wech is required to connect both core proteins of the linker complex during embryonic muscle attachment. Both the NHL and the B-box/coiled-coil domains of Wech are required for proper interaction with Talin and ILK. The single murine Wech orthologue is also colocalized with Talin and ILK in muscle tissue. We propose that Wech proteins are crucial and evolutionarily conserved regulators of the integrin-cytoskeleton link.
Impact Factor
Scopus SNIP
Web of Science
Times Cited
Scopus
Cited By
Altmetric
17.623
3.530
40
49
Tags
Anmerkungen
Besondere Publikation
Auf Hompepage verbergern

Zusatzinfos bearbeiten
Eigene Tags bearbeiten
Privat
Eigene Anmerkung bearbeiten
Privat
Auf Publikationslisten für
Homepage nicht anzeigen
Als besondere Publikation
markieren
Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Sprache englisch
Veröffentlichungsjahr 2008
HGF-Berichtsjahr 2008
ISSN (print) / ISBN 1465-7392
e-ISSN 1476-4679
Zeitschrift Nature Cell Biology
Quellenangaben Band: 10, Heft: 4, Seiten: 422-428 Artikelnummer: , Supplement: ,
Verlag Nature Publishing Group
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Molecular Immunology (IMI)
PSP-Element(e) G-501700-003
DOI 10.1038/ncb1704
Scopus ID 43049110021
Erfassungsdatum 2008-11-21
[➜Korrektur melden]