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Truncated CASK does not alter skeletal muscle or protein interactors
Author(s) -
Sanford Jamie L.,
Mays Tessily A.,
Varian Kenneth D.,
Wilson Joanna B.,
Janssen Paul M.L.,
RafaelFortney Jill A.
Publication year - 2008
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.20993
Subject(s) - cask , skeletal muscle , microbiology and biotechnology , neuromuscular junction , biology , myocyte , anatomy , neuroscience , genetics
Abstract CASK (Ca 2+ , calmodulin‐associated serine/threonine kinase) is an essential mammalian cell junction protein and is also crucial at Drosophila neuromuscular synapses. We have shown that CASK is present in mammalian skeletal muscle at the postsynaptic membrane of the neuromuscular junction. CASK interacts biochemically with channels at central synapses, and studies in cultured cells have led to proposed functions for CASK. However, in vivo functions of CASK in skeletal muscle remain unknown. To test hypotheses of CASK functions, we generated two lines of transgenic mice, which overexpress full‐length and truncated CASK protein in skeletal muscle. Extensive analyses showed that overexpression of CASK protein did not affect the morphology or physiology of skeletal muscle, the morphology of the neuromuscular junction, or the levels or distribution of protein interactors. These results contrast with previous cell culture experiments and emphasize the importance of in vivo analysis of protein function. Muscle Nerve, 2008