The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Cask  -  calcium/calmodulin-dependent serine...

Mus musculus

Synonyms: Calcium/calmodulin-dependent serine protein kinase, DXPri1, DXRib1, LIN-2, Pals3, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Cask

  • The importance of mLin-2/CASK in mammalian development is demonstrated by the fact that mutations in mLin-2/CASK or SAP97, another MAGUK protein, lead to cleft palate in mice [1].

High impact information on Cask

  • Our data identify evolutionarily conserved protein-protein interaction domains that link mLin-2/CASK to SAP97 and account for their common phenotype when mutated in mice [1].
  • In this report, we further define the binding of the L27C domain of mLin-2/CASK to the L27 domain of mLin-7 and identify the binding partner for L27N of mLin-2/CASK [1].
  • In Caenorhabditis elegans, a complex of three PDZ proteins, LIN-2/7/10, mediates basolateral targeting of a receptor tyrosine kinase [2].
  • Here, we report that X11alpha directly binds to the mammalian homologue of Lin-2 (mLin-2), also known as CASK [3].

Other interactions of Cask

  • This binding is mediated by direct interaction between the Calmodulin Kinase II (CKII)-like domain of mLin-2 and the amino terminus of X11alpha [3].
  • Furthermore, we can detect direct interactions between mLin-2 and mammalian Lin-7 (mLin-7) [3].


  1. A novel and conserved protein-protein interaction domain of mammalian Lin-2/CASK binds and recruits SAP97 to the lateral surface of epithelia. Lee, S., Fan, S., Makarova, O., Straight, S., Margolis, B. Mol. Cell. Biol. (2002) [Pubmed]
  2. Contrasting localizations of MALS/LIN-7 PDZ proteins in brain and molecular compensation in knockout mice. Misawa, H., Kawasaki, Y., Mellor, J., Sweeney, N., Jo, K., Nicoll, R.A., Bredt, D.S. J. Biol. Chem. (2001) [Pubmed]
  3. Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting. Borg, J.P., Straight, S.W., Kaech, S.M., de Taddéo-Borg, M., Kroon, D.E., Karnak, D., Turner, R.S., Kim, S.K., Margolis, B. J. Biol. Chem. (1998) [Pubmed]
WikiGenes - Universities