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Novel role of bHLH protein Daughterless in synaptogenesis
Author(s) -
Robinson Erin L,
Waddell Edward A,
D'Rozario Mitchell,
Marenda Daniel R
Publication year - 2016
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.30.1_supplement.869.7
Subject(s) - synaptogenesis , microbiology and biotechnology , biology , transcription factor , neurexin , transcription (linguistics) , drosophila melanogaster , function (biology) , mef2 , basic helix loop helix , dna binding protein , genetics , enhancer , gene , linguistics , philosophy , receptor , postsynaptic potential
Basic Helix Loop Helix (bHLH)proteins are a class of highly conserved transcription factors. Proneural bHLH proteins have been extensively studied for their role in neurogenesisregulation, however the role of class 1 bHLH proteins in postmitotic cells remains unknown. Class 1 bHLH proteins function by heterodimerizing with class II or V bHLH proteins, orhomodimerizing to alter transcription. Ourlab has identified a novel role of the class 1 bHLH protein, Daughterless (Da),in postmitotic neurons in Drosophila Melanogaster, in which it restricts synaptogenesis. Here, we show that Da performs this function in part through restricting Neurexin expression, a cell adhesion protein. Our data also suggests that Da cooperates with the class V bHLH protein, Extramacrochaetae (Emc), in postmitotic neurons. Emc is a well‐established binding partner of Da during development, where it serves to sequester Da, preventing DNA binding. Taken together, these results provide a novel role for the class 1 bHLH protein, Daughterless, in postmitotic neurons.