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Rodina proteinů obsahujících sterol-sensing doménu
Ditrychová, Karolína ; Zíková, Martina (advisor) ; Fafílek, Bohumil (referee)
1. Abstract Sterol sensing domain (SSD) is a putative transmembrane region consisting of 5 helices and in few cases it was shown that it interacts with cholesterol. Proteins containing this domain play a role in many cellular pathways connected to cholesterol. It was first described in a study of 3-hydroxy-3-methylglutaryl-CoA reductase (HMG-CoA reductase). It is an enzyme playing role in cholesterol biosynthesis and its transcription is regulated by sterol regulatory element binding protein cleavage activating protein (SCAP). HMG-CoA reductase and SCAP were the first proteins where SSD was recognized. After that, other proteins were described; one more protein functioning in cholesterol biosynthesis was described as containing SSD - 7-dehydrocholesterol reductase. Also two proteins playing role in cholesterol endocytosis - Niemann-Pick type C 1 liked 1 - and in its efflux from lysosomes - Niemann-Pick type C 1 - were recognized. Furthermore, proteins playing role in Hedgehog signalling Patched, Patched-related and Dispatched were found as SSD containing structures. In the end, tumour-suppressor gene TRC8 was also recognized as member of SSD family. In this text, structure and function of these proteins is summarized. Key words: sterol sensing domain, Hedgehog signalling pathway, sterol binding protein,...
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