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N-Glycosylation is required for FDNC5 stabilization and irisin secretion
Yongwei Nie1,2, Dongjun Liu3
1The Key Laboratory of China Education Ministry for Research of Mammal Reproductive Biology and Biotechnology, School of Life Sciences, Inner Mongolia University, Hohhot 010020, China.
The Biochemical Journal
|July 23, 2017
Summary
Irisin secretion is modulated by N-glycosylation of FNDC5. This study reveals that N-glycosylation impacts irisin release, offering new insights into glycosylated irisin secretion and FNDC5 stability.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Irisin, a myokine from FNDC5, mediates thermogenesis in white adipose tissue.
- The role of N-glycosylation in FNDC5 function and irisin secretion is not well understood.
- Previous biochemical data suggested N-glycosylation does not affect irisin's ligand or receptor activation.
Purpose of the Study:
- To investigate the N-glycosylation sites of FNDC5.
- To determine the impact of N-glycosylation on irisin secretion.
- To understand the regulation of irisin secretion.
Main Methods:
- Analysis of potential N-glycosylation sites on FNDC5.
- Assessment of irisin secretion in the presence and absence of N-glycosylation.
- Evaluation of FNDC5 expression levels following myoblast differentiation.
Main Results:
- Identified two potential N-glycosylation sites (Asn36 and Asn81) on FNDC5 that can be occupied by N-glycans.
- Demonstrated that the absence of N-glycosylation reduces irisin secretion, linked to FNDC5 instability and signal peptide cleavage deficiency.
- Observed increased expression of N-glycosylated FNDC5 after myoblast differentiation.
Conclusions:
- N-glycosylation plays a crucial role in modulating the secretion of irisin.
- Understanding the N-glycosylation of FNDC5 enhances knowledge of irisin secretion mechanisms.
- This study provides novel insights into the regulation of glycosylated irisin release.
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