期刊
JOURNAL OF CELL SCIENCE
卷 127, 期 17, 页码 3794-3804出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.150334
关键词
skNAC; Smyd1; m-Bop; Mms21; Nse2; Sumoylation; Myogenic differentiation
类别
资金
- Deutsche Forschungsgemeinschaft [Myograd] [GRK1631]
- German Foundation for Cardiac Research (DSHF)
- German Research Foundation (DFG) [Mu 1556 5-1]
- Tubingen University Medical Clinic
- Friede-Springer-Herz-Stiftung
Skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC; encoded by NACA) is exclusively found in striated muscle cells. Its function, however, is largely unknown. Previous reports have demonstrated that skNAC binds to m-Bop/Smyd1, a multi-functional protein that regulates myogenesis both through the control of transcription and the modulation of sarcomerogenesis, and that both proteins undergo nuclear-to-cytoplasmic translocation at the later stages of myogenic differentiation. Here, we show that skNAC binds to the E3 SUMO ligase mammalian Mms21/Nse2 and that knockdown of Nse2 expression inhibits specific aspects of myogenic differentiation, accompanied by a partial blockade of the nuclear-to-cytoplasmic translocation of the skNAC-Smyd1 complex, retention of the complex in promyelocytic leukemia (PML)-like nuclear bodies and disturbed sarcomerogenesis. In addition, we show that the skNAC interaction partner Smyd1 contains a putative sumoylation motif and is sumoylated in muscle cells, with depletion of Mms21/Nse2 leading to reduced concentrations of sumoylated Smyd1. Taken together, our data suggest that the function, specifically the balance between the nuclear and cytosolic roles, of the skNAC-Smyd1 complex might be regulated by sumoylation.
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