Phosphorylation on TRPV4 Serine Residue 824 Enhances Its Association with PGM1
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چکیده
منابع مشابه
Phosphorylation on TRPV4 Serine Residue 824 Enhances Its Association with PGM1
The TRPV4 cation channel is expressed in a broad range of tissues and participates in the generation of a Ca2+ signal and/or depolarization of membrane potential. Here, human phosphoglucomutase-1 (PGM1), an enzyme that converts glucose-6 phosphate to glucose-1 phosphate in the glycolysis pathway, as the first auxiliary protein of TRPV4 Ca2+ channels, is identified with yeast two hybrid system, ...
متن کاملPhosphorylation on TRPV4 Serine 824 Regulates Interaction with STIM1
The TRPV4 cation channel, a member of the TRP vanilloid subfamily, is expressed in a broad range of tissues where it participates in the generation of a Ca2+ signal and/or depolarization of membrane potential. Here, we identified stromal interaction molecule 1 precursor (STIM1) as an auxiliary protein of this epithelial Ca2+channel using confocal microscopy analysis and GST pull-down assay. The...
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Phosphorylation by CK2 and MAPK enhances calnexin association with ribosomes.
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ژورنال
عنوان ژورنال: American Journal of Molecular Biology
سال: 2016
ISSN: 2161-6620,2161-6663
DOI: 10.4236/ajmb.2016.61004