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Characterization of a Novel Scaffold Protein Involved in Skeletal Muscle Differentiation
Author(s) -
Takahashi Mark,
Virtanen Carl,
Paris James
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.6.lb10-a
Subject(s) - scaffold protein , c2c12 , microbiology and biotechnology , biology , transcription factor , mef2c , signal transduction , mef2 , skeletal muscle , cellular differentiation , gene knockdown , pi3k/akt/mtor pathway , myocyte , myogenesis , genetics , gene , anatomy , enhancer
The phosphatidylinositol 3‐kinase (PI 3 K) signaling pathway has been associated with a variety of cellular functions, ranging from cell cycle regulation to tissue development. Altered or deviant signaling through this cascade has been associated with a number of cancers and disorders. Although years of research have extensively characterized this signaling pathway, not all aspects of it have been fully elucidated. Here we show a novel plekstrin homology domain containing protein is also involved in this pathway. This protein was identified during a screen of MEF2 transcription factor binding sites during skeletal muscle differentiation. The protein is a well‐conserved, though previously uncharacterized, protein found in a variety of sequenced tetrapods. Association analysis demonstrated that the protein binds specifically to PI 3 K signaling pathway members. In C 2 C 12 myoblast cells prior to differentiation, the protein was localized to the cytosol, migrating to the membrane following initiation of muscle differentiation. Knockdown by RNAi resulted in inhibition of myotube formation. Finally, mRNA levels were found to be differentially regulated across a number of tumour pathologies.