Letter abstract
Nature Cell Biology 10, 422 - 428 (2008)
Published online: 9 March 2008 | doi:10.1038/ncb1704
The NHL-domain protein Wech is crucial for the integrin–cytoskeleton link
Birgit Löer1, Reinhard Bauer1, Roland Bornheim2, Jessica Grell2, Elisabeth Kremmer3, Waldemar Kolanus2 & Michael Hoch1
Integrin transmembrane receptors mediate cell adhesion through intracellular linker proteins that connect to the cytoskeleton1, 2. 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 family3 members, and an NHL domain4. In
-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.
- Life and Medical Sciences Institute (LIMES), Program Unit Development & Genetics, Laboratory for Molecular Developmental Biology, University of Bonn, Meckenheimer Allee 169, D-53115 Bonn, Germany.
- LIMES-Institute, Program Unit Molecular Cell and Immune Biology, Laboratory for Molecular Immunology, University of Bonn, Karlrobert-Kreiten-Str.13, D-53115 Bonn, Germany.
- Helmholtz Zentrum München, Institut für Molekulare Immunologie, Marchioninistr. 25, 81377 München, Germany.
Correspondence to: Michael Hoch1 e-mail: m.hoch@uni-bonn.de
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
RESEARCH
Functional consequences of integrin-linked kinase activation in podocyte damageKidney International Original Article
Integrin-dependent anchoring of a stem-cell nicheNature Cell Biology Letter (01 Dec 2007)
See all 5 matches for Research
