کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1926702 | 1536467 | 2008 | 10 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Identification and characterization of the ER/lipid droplet-targeting sequence in 17β-hydroxysteroid dehydrogenase type 11 Identification and characterization of the ER/lipid droplet-targeting sequence in 17β-hydroxysteroid dehydrogenase type 11](/preview/png/1926702.png)
17β-Hydroxysteroid dehydrogenase type 11 (17βHSD11) is mostly localized on the endoplasmic reticulum (ER) membrane under normal conditions and redistributes to lipid droplets (LDs) when the formation of LDs is induced. In this study, confocal microscopy analyses of the subcellular localization of the mutated 17βHSD11 proteins in cells with or without LDs revealed that both an N-terminal hydrophobic sequence and an adjacent sequence that has a weak homology with the PAT motif are independently necessary and both parts together (28 amino acid residues in total) are sufficient for the dual localization of 17βHSD11. Mutation analyses suggest that the PAT-like motif in 17βHSD11 will not be functionally similar to the canonical PAT motif. Hsp60 was identified as a possibly interacting protein with the PAT-like motif, and biochemical and microscopic analyses suggest that Hsp60 may be partly, but not necessarily involved in recognition of the PAT-like part of the targeting sequence of 17βHSD11.
Journal: Archives of Biochemistry and Biophysics - Volume 479, Issue 2, 15 November 2008, Pages 121–130