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首页> 外文期刊>Journal of cellular biochemistry. >Cytoskeletal protein vimentin interacts with and regulates peroxisome proliferator-activated receptor gamma via a proteasomal degradation process
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Cytoskeletal protein vimentin interacts with and regulates peroxisome proliferator-activated receptor gamma via a proteasomal degradation process

机译：细胞骨架蛋白波形蛋白通过蛋白酶体降解过程与过氧化物酶体增殖物激活的受体γ相互作用并对其进行调节

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摘要

Peroxisome proliferators-activated receptor gamma (PPARγ) receptor is a transcription factor that is located in and functions primarily in the nucleus. PPARγ is exported from the nucleus upon mitogen and ligand stimulation under certain circumstances. However, a cytoplasmic PPARγ interacting protein and its function have not been previously identified. Here, we report for the first time that cytosolic PPARγ interacts directly with cytoskeletal vimentin. We performed PPARγ immunoprecipitation followed by mass spectrometry to identify the vimentin-PPARγ complex. This interaction was confirmed by reciprocal vimentin and PPARγ immunoprecipitation and co-immunofluorescence examination. We demonstrated that PPARγ colocalized with vimentin in certain organelles that is golgi, mitochondria, and endoplasmic reticulum. In cells depleted of vimentin, PPARγ was ubiquitinated and targeted to a proteasomal degradation pathway. Together, these findings indicate a direct interaction of PPARγ with vimentin in the cytosolic compartment, in which vimentin appears to play a role in regulating the turnover rate of PPARγ, which may further regulate genomic or non-genomic activities through the regulation of PPARγ protein degradation.
机译：过氧化物酶体增殖物激活受体γ（PPARγ）受体是位于细胞核中并主要在细胞核中起作用的转录因子。在某些情况下，在有丝分裂原和配体刺激下，PPARγ从细胞核中输出。但是，胞浆中的PPARγ相互作用蛋白及其功能尚未得到鉴定。在这里，我们首次报道胞质PPARγ与细胞骨架波形蛋白直接相互作用。我们进行了PPARγ免疫沉淀，然后进行质谱分析以鉴定波形蛋白-PPARγ复合物。相互波形蛋白和PPARγ免疫沉淀以及免疫荧光检测证实了这种相互作用。我们证明了PPARγ与波形蛋白在某些细胞器（高尔基体，线粒体和内质网）中共定位。在缺乏波形蛋白的细胞中，PPARγ被泛素化并靶向蛋白酶体降解途径。在一起，这些发现表明PPARγ与波形蛋白在胞浆区室中直接相互作用，其中波形蛋白似乎在调节PPARγ的周转率中起作用，这可能通过调节PPARγ蛋白降解来进一步调节基因组或非基因组活性。

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