TAILIEUCHUNG - Báo cáo khoa học: SREBPs: protein interaction and SREBPs Ryuichiro Sato

Sterol regulatory element-binding proteins (SREBPs) are tightly controlled by various mechanisms, including intracellular localization, protein process-ing, limited proteolysis, post-translational modifications and interaction with associated proteins. Here, I review the regulatory mechanisms of SREBP activity through the interaction with various kinds of protein. | MINIREVIEW SREBPs protein interaction and SREBPs Ryuichiro Sato Department of Applied BiologicalChemistry Graduate Schoolof Agriculturaland Life Sciences University of Tokyo Japan Keywords AtF6 HNF-4 importin LRH-1 PGC-1 S1P S2P SCAP SREBPs Sterol regulatory element-binding proteins SREBPs are tightly controlled by various mechanisms including intracellular localization protein processing limited proteolysis post-translational modifications and interaction Correspondence R. Sato Department of Applied Biological Chemistry Graduate Schoolof Agricultural and Life Sciences The University of Tokyo Tokyo 113-8657 Japan Fax 81 3 5841 5136 Tel 81 3 5841 8029 E-mail aroysato@ with associated proteins. Here I review the regulatory mechanisms of SREBP activity through the interaction with various kinds of protein. Received 6 August 2008 revised 22 October 2008 accepted 24 October 2008 doi Introduction The sterol regulatory element-binding protein SREBP family members SREBP-1 and SREBP-2 are localized on the endoplasmic reticulum ER as membrane proteins after being synthesized. Once the intracellular cholesterol level is decreased the SREBPs subsequently move in vesicles to the Golgi complex where they are processed sequentially by two proteases. These cleavage steps release the mature forms of SREBPs which enter the nucleus and activate genes related to cholesterol and fatty acid metabolism 1 2 . In both the cytoplasm and nucleus SREBPs associate with a variety of proteins. This interaction determines their intracellular translocation and stability and also regulates their activities as transcriptional factors. Protein interaction on the ER and in the cytosol SREBPs are localized on the ER membrane associating with another ER membrane protein SREBP cleavage-activating protein SCAP Fig. 1 . SCAP has two distinct domains. The N-terminal domain has eight transmembrane helices which include the so-called sterol-sensing .

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