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
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DOI：
10.1016/j.abb.2008.08.020
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发表时间：
2008-11-15
影响因子：
3.9
通讯作者：
Motojima, Kiyoto
中科院分区：
文献类型：
--
作者：
Horiguchi, Yuka;Araki, Makoto;Motojima, Kiyoto
17 β-羟基类固醇脱氢酶11型（17 β HSD 11）在正常条件下主要定位于内质网（ER）膜上，并在诱导形成脂滴（LD）时重新分布至LD。在这项研究中，在有或没有LD的细胞中突变的17 β HSD 11蛋白的亚细胞定位的共聚焦显微镜分析显示，N-末端疏水序列和与PAT基序具有弱同源性的相邻序列都是独立必需的，并且这两个部分一起（总共28个氨基酸残基）足以用于17 β HSD 11的双重定位。突变分析表明，在17 β HSD 11的PAT样基序将不会在功能上类似于典型的PAT基序。Hsp 60被鉴定为可能与PAT样基序相互作用的蛋白质，生物化学和显微镜分析表明，Hsp 60可能部分但不一定参与识别17 β HSD 11靶向序列的PAT样部分。(C)2008年爱思唯尔公司All rights reserved.
17P-Hydroxysteroid dehydrogenase type 11 (17 beta HSD11) 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 17 beta HSD11 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 17 beta HSD11. Mutation analyses suggest that the PAT-like motif in 17 beta HSD11 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 17 beta HSD11. (C) 2008 Elsevier Inc. All rights reserved.