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Galectin‐8 Regulates Primary Cilia Assembly and Contacts Development
Author(s) -
Syu JhanJhang,
Jou Tzuu-Shuh
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2020.34.s1.09099
Subject(s) - ciliogenesis , cilium , microbiology and biotechnology , galectin , chemistry , respiratory epithelium , biology , organelle , epithelium , genetics
Primary cilium is a significant sensory organelle protruding from cellular surface to sense and thereby transduce environmental clues. A critical aspect of cilium morphology is defined by its length and contact formation between neighboring cilia. Galectins are a group of β‐galactoside‐binding animal lectins found both in the cytosol, and secreted in the extracellular space through unconventional pathway. Galectin‐8 (Gal‐8) is a protein with 2 tandem‐repeat carbohydrate recognizing domains (CRDs), and a high affinity of its N‐terminal CRD for sialylated or sulfated glycoconjugates which distinguishes it from other galectins. We found that knockdown of endogenous Gal‐8 inhibited primary ciliogenesis in polarized Madin‐Darby canine kidney (MDCK) cells, and both endogenous and epitope‐tagged Gal‐8s were noted at the surface of primary cilia. Furthermore, application of purified recombinant Gal‐8 protein at sub‐micromolar concentration to the apical, but not to the basolateral domain, resulted in growth and adhesion of PC in polarized MDCK cells within minutes. To identify the putative binding partner at the cilia surface for Gal‐8, we exploited a strategy applying surface biotinylation and surface pull‐down followed by proteomic assay. With these approaches, we found out several potential candidates and would examine their roles in ciliogenesis by engineering gene‐editing mutant cell lines for future study.