Glycogen synthase kinase-3-mediated phosphorylation of serine 73 targets sterol response element binding protein-1c (SREBP-1c) for proteasomal degradation | Zendy

Qingming Dong | Zendy; Francesco Giorgianni | Zendy; Šárka Beranová-Giorgianni | Zendy; Xiong Deng | Zendy; Robert N. O’Meally | Zendy; Dave Bridges | Zendy; Edwards A. Park | Zendy; Robert N. Cole | Zendy; Marshall B. Elam | Zendy; Rajendra Raghow | Zendy

Open Access

Glycogen synthase kinase-3-mediated phosphorylation of serine 73 targets sterol response element binding protein-1c (SREBP-1c) for proteasomal degradation

Author(s) -

Qingming Dong,

Francesco Giorgianni,

Šárka Beranová-Giorgianni,

Xiong Deng,

Robert N. O’Meally,

Dave Bridges,

Edwards A. Park,

Robert N. Cole,

Marshall B. Elam,

Rajendra Raghow

Publication year - 2015

Publication title -

bioscience reports

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.938

H-Index - 77

eISSN - 1573-4935

pISSN - 0144-8463

DOI - 10.1042/bsr20150234

Subject(s) - sterol regulatory element binding protein , phosphorylation , serine , gsk 3 , gsk3b , biochemistry , glycogen synthase , biology , phosphorylation cascade , kinase , protein kinase a , phosphoserine , transactivation , chemistry , protein phosphorylation , microbiology and biotechnology , transcription factor , gene

We have identified Serine 73 as a novel GSK-3β site on SREBP-1c that alters its affinity for SCAP, and proteasomal degradation. Phosphorylation of Serine 73 by GSK-3β during starvation (insulin-depleted stat) may lead to lower levels of SREBP-1c; conversely, de-phosphorylation of this site may be involved in stabilizing SREBP-1c by insulin (by blocking GSK-3β action). A functional role of this site needs to be corroborated in vivo .

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