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Identification of TRPP2 binding partners in mice tissues
Author(s) -
Ng Courtney,
Yu Yong
Publication year - 2017
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.31.1_supplement.772.6
Subject(s) - autosomal dominant polycystic kidney disease , transient receptor potential channel , pkd1 , biology , trpc1 , ion channel , intracellular , microbiology and biotechnology , receptor , computational biology , genetics , kidney
Mutations in transient receptor potential polycystin‐2 (TRPP2 or PC2) and its related protein, polycystin‐1 (PKD1 or PC1) result in autosomal dominant polycystic kidney disease (ADPKD), one of the most common human genetic diseases. TRPP2 and PKD1 form a receptor/ion channel complex, which has been proposed to function in coupling extracellular stimuli to intracellular Ca 2+ signals. The study of these proteins is essential to understanding the characteristics of this channelopathy and developing specific treatments. Our focus has been working with TRPP2 in order to gain insight on the molecular mechanisms of its structural assembly, and channel function and regulation. TRP channels are localized in a variety of tissues and perform specific roles in sensory physiology. Specifically, TRPP2 is known to express in the human heart, brain, kidney, lung, testis, and ovary. It is also known to have direct binding to a number of proteins, many of which are involved in cytoskeletal association, trafficking and ion channel modulation. The intracellular C‐terminus of TRPP2 has been shown to be involved in the association of some of these binding partners. We believe that the C‐terminus of TRPP2 has major implications in diversifying its role in different tissue types. The approach taken here was to identify novel TRPP2 C‐terminal binding partners present in different tissue types. We purified the C‐terminus of human TRPP2 by expressing it in E. coli , and used it to pull‐down these possible binding partners in several mice tissues, including the brain, kidneys, heart, lungs, and liver. Potential partners were isolated and mass spectrometry was used to identify these proteins for further analysis and functional study. The results of this study will shed light on the specific physiological function of TRPP2 in particular organs. Support or Funding Information This research is funded NIH Grant DK102092.