7/30/2023 0 Comments Multipass protein![]() ![]() The experimental study was performed in compliance with the laws of the People's Republic of China. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.įunding: This work was supported by grants from the National Important Research Plan of China (2011CB944302), grant for the youth (81101855) from the National Natural Science Foundation of China, the State Key Laboratory Special fund (2060204) from the Ministry of Science, and the Research Fund for the Doctoral Program of High Education (20111106110023). Received: JAccepted: ApPublished: May 18, 2012Ĭopyright: © 2012 Wan et al. PLoS ONE 7(5):Įditor: Anna Tramontano, University of Rome, Italy Taken together, our findings suggest that RHBDD1 is involved in the regulation of a nonclassical exosomal secretion pathway through the restriction of TSAP6.Ĭitation: Wan C, Fu J, Wang Y, Miao S, Song W, Wang L (2012) Exosome-Related Multi-Pass Transmembrane Protein TSAP6 Is a Target of Rhomboid Protease RHBDD1-Induced Proteolysis. We found that the increase in FasL and Trail increased exosome-induced apoptosis in Jurkat cells. In addition, the elevation of exosome secretion by RHBDD1 inactivation was reduced when TSAP6 was knocked down, indicating that the role of RHBDD1 in regulating exosomal trafficking is very likely to be TSAP6-dependent. The increased exosome secretion was verfied through the detection of certain exosomal components, including Tsg101, Tf-R, FasL and Trail. Exosome secretion was significantly elevated when RHBDD1 was inactivated in the two cells lines. A somatic cell knock-in approach was used to genetically inactivate the endogenous RHBDD1 in HCT116 and RKO colon cancer cells. In addition, mass spectrometry and mutagenesis analyses both indicated that the major cleavage site laid in the C-terminal of the third transmembrane domain of TSAP6. The cleavage of TSAP6 was not restricted to its glycosylated form and occurred in three different regions. RHBDD1 was found to induce the proteolysis of TSAP6 in a dose- and activity-dependent manner. In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1. We have previously reported that rhomboid domain containing 1 (RHBDD1), a mammalian rhomboid protease highly expressed in the testis, can cleave the Bcl-2 protein Bik. ![]()
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