Post-translational modifications and secretion
of Wnt proteins

Yanqin Lu; Xiuzh Ren; YanzhouWang; Jinxiang Han

doi:10.26717/BJSTR.2018.09.001824

Review ArticleOpen Access

Post-translational modifications and secretion of Wnt proteins

Volume 9 - Issue 4

**Yanqin Lu^1,2*, Xiuzh Ren³, YanzhouWang⁴ and Jinxiang Han^1,2**

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- ¹Key Laboratory for Biotech-Drugs Ministry of Health, Key Laboratory for Rare & Uncommon Diseases of Shandong Province, Shandong Medicinal Biotechnology Centre, Shandong Academy of Medical Sciences, China
- ²School of Medicine and Life Sciences, University of Jinan-Shandong Academy of Medical Sciences, China
- ³Department of Orthopedic Surgery, The People’s Hospital of Wuqing District, China
- ⁴Department of Orthopedic Surgery, Shandong Provincial Hospital, China
*Corresponding author: Yanqin Lu, Key Laboratory for Biotech-Drugs Ministry of Health, Key Laboratory for Rare & Uncommon Diseases of Shandong Province, Shandong Medicinal Biotechnology Centre, Shandong Academy of Medical Sciences, China

Received: September 28, 2018; Published: October 04, 2018

DOI: 10.26717/BJSTR.2018.09.001824

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Abstract

Wnts are secreted lipid-modified glycoproteins in most mammalian genomes. Wnt ligands are the essential components of Wnt signaling pathways. Before binding to specific receptors, Wnt proteins experienced post-translational modification of acylation and N-glycosylation mediated by acyltransferase porcupine. Mature Wnts are transported from the Golgi to plasma membrane under association with Wntless. Retromer complex, P24 and other molecules are all involved in the secretion and release of Wnts. In this review, we provide an update of the post-translational modification, secretion and release of Wnts.

Keywords: Wnts; Acylation; N glycosylation; Wntless; Retromer

Abstract | Introduction | Acknowledgement| References|