FKBP8 enhances protein stability of the CLC-1 chloride channel at the plasma membrane

Yi Jheng Peng, Yi Ching Lee, Ssu Ju Fu, Yun Chia Chien, Yi Fan Liao, Tsung Yu Chen, Chung Jiuan Jeng*, Chih Yung Tang


研究成果: Article同行評審

6 引文 斯高帕斯(Scopus)


Mutations in the skeletal muscle-specific CLC-1 chloride channel are associated with the human hereditary disease myotonia congenita. The molecular pathophysiology underlying some of the disease-causing mutations can be ascribed to defective human CLC-1 protein biosynthesis. CLC-1 protein folding is assisted by several molecular chaperones and co-chaperones, including FK506-binding protein 8 (FKBP8). FKBP8 is generally considered an endoplasmic reticulum-and mitochondrion-resident membrane protein, but is not thought to contribute to protein quality control at the cell surface. Herein, we aim to test the hypothesis that FKBP8 may regulate CLC-1 protein at the plasma membrane. Surface biotinylation and subcellular fractionation analyses reveal that a portion of FKBP8 is present at the plasma membrane, and that co-expression with CLC-1 enhances surface localization of FKBP8. Immunoblotting analyses of plasma membrane proteins purified from skeletal muscle further confirm surface localization of FKBP8. Importantly, FKBP8 promotes CLC-1 protein stability at the plasma membrane. Together, our data underscore the importance of FKBP8 in the peripheral quality control of CLC-1 channel.

期刊International Journal Of Molecular Sciences
出版狀態Published - 12月 2018


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