Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 497, Issue 1, Pages 194-199Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2018.02.053
Keywords
Protein kinase A; CREB; O-GlcNAcylation; Phosphorylation
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Funding
- Nantong University
- New York State Office for People with Developmental Disabilities (OPWDD)
- National Natural Science Foundation of China [31671046, 81300978]
- China Scholarship Council [201608110204]
- Undergraduate Training Program for Innovation and Entrepreneurship of Jiangsu Province [201710304113X]
- Neural Regeneration Co-innovation Center of Jiangsu Province
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O-GlcNAcylation is a post-translational modification of proteins. Protein kinase A (PKA)-cAMP response element binding protein (CREB) signaling plays critical roles in multiple biological processes. Isoforms alpha and beta of PICA catalytic subunit (PKAc) and CREB are modified by O-GlcNAcylation. In the present study, we determined the role of O-GlcNAcylation in PKAc isoform-specific CREB signaling. We found that up regulation of O-GlcNAcylation enhanced CREB phosphorylation, but suppressed CREB expression in exogenous PKAc isoform-unspecific manner. PKAc isoforms affected exogenous expression of OGT or OGA and protein O-GlcNAcylation differently. Up-regulation of O-GlcNAcylation did not significantly affect net PKAc alpha-CREB signaling, but enhanced PKAc beta-CREB signaling. The role of O-GlcNAcylation in PKA-CREB signaling was desensitized by insulin treatment. This study suggests a role of O-GlcNAcylation in PKA-CREB signaling by affecting phosphorylation of CREB in a PKAc isoform-specific manner. (C) 2018 Elsevier Inc. All rights reserved.
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