Aufgrund von Vorbereitungen auf eine neue Version von KOPS, können am Montag, 6.2. und Dienstag, 7.2. keine Publikationen eingereicht werden. (Due to preparations for a new version of KOPS, no publications can be submitted on Monday, Feb. 6 and Tuesday, Feb. 7.)
Type of Publication: | Journal article |
Publication status: | Published |
URI (citable link): | http://nbn-resolving.de/urn:nbn:de:bsz:352-2-1u26sdbgr8lu30 |
Author: | Yatsenko, Andriy S.; Kucherenko, Mariya M.; Pantoja, Mario; Fischer, Kevin A.; Madeoy, Jennifer; Deng, Wu-Min; Schneider, M.; Baumgartner, Stefan; Shcherbata, Halyna; Ruohola-Baker, Hannele et al. |
Year of publication: | 2009 |
Published in: | BMC Developmental Biology ; 9 (2009), 1. - 18. - BioMed Central. - eISSN 1471-213X |
DOI (citable link): | https://dx.doi.org/10.1186/1471-213X-9-18 |
Summary: |
Background
Dystroglycan (Dg) is a transmembrane protein that is a part of the Dystrophin Glycoprotein Complex (DGC) which connects the extracellular matrix to the actin cytoskeleton. The C-terminal end of Dg contains a number of putative SH3, SH2 and WW domain binding sites. The most C-terminal PPXY motif has been established as a binding site for Dystrophin (Dys) WW-domain. However, our previous studies indicate that both Dystroglycan PPXY motives, WWbsI and WWbsII can bind Dystrophin protein in vitro. Results We now find that both WW binding sites are important for maintaining full Dg function in the establishment of oocyte polarity in Drosophila. If either WW binding site is mutated, the Dg protein can still be active. However, simultaneous mutations in both WW binding sites abolish the Dg activities in both overexpression and loss-of-function oocyte polarity assays in vivo. Additionally, sequence comparisons of WW binding sites in 12 species of Drosophila, as well as in humans, reveal a high level of conservation. This preservation throughout evolution supports the idea that both WW binding sites are functionally required. Conclusion Based on the obtained results we propose that the presence of the two WW binding sites in Dystroglycan secures the essential interaction between Dg and Dys and might further provide additional regulation for the cytoskeletal interactions of this complex. |
Subject (DDC): | 570 Biosciences, Biology |
Keywords: | Muscular Dystrophy, Follicle Cell, Germline Cell, Oocyte Nucleus, Cellular Polarity |
Link to License: | Attribution 2.0 Generic |
Refereed: | Yes |
YATSENKO, Andriy S., Mariya M. KUCHERENKO, Mario PANTOJA, Kevin A. FISCHER, Jennifer MADEOY, Wu-Min DENG, M. SCHNEIDER, Stefan BAUMGARTNER, Halyna SHCHERBATA, Hannele RUOHOLA-BAKER, 2009. The conserved WW-domain binding sites in Dystroglycan C-terminus are essential but partially redundant for Dystroglycan function. In: BMC Developmental Biology. BioMed Central. 9(1), 18. eISSN 1471-213X. Available under: doi: 10.1186/1471-213X-9-18
@article{Yatsenko2009conse-50998, title={The conserved WW-domain binding sites in Dystroglycan C-terminus are essential but partially redundant for Dystroglycan function}, year={2009}, doi={10.1186/1471-213X-9-18}, number={1}, volume={9}, journal={BMC Developmental Biology}, author={Yatsenko, Andriy S. and Kucherenko, Mariya M. and Pantoja, Mario and Fischer, Kevin A. and Madeoy, Jennifer and Deng, Wu-Min and Schneider, M. and Baumgartner, Stefan and Shcherbata, Halyna and Ruohola-Baker, Hannele}, note={Article Number: 18} }
Yatsenko_2-1u26sdbgr8lu30.pdf | 134 |