Sterol regulatory element-binding protein

（重定向自SREBP）

SREBP activation by proteolytic cleavage. SREBP precursors are retained in the ER membranes through a tight association with SCAP and a protein of the INSIG family. Under the appropriate conditions, SCAP dissociates from INSIG and escorts the SREBP precursors from the ER to the Golgi apparatus. Once there, two proteases, S1P and S2P, sequentially cleave the precursor protein, releasing the mature form of SREBPs into the cytoplasm. The mature form then migrates to the nucleus, where it activates the promoter of genes involved in cholesterol uptake or in cholesterol synthesis. SREBP processing can be controlled by the cellular sterol content.

Sterol regulatory element-binding proteins (SREBPs) are transcription factors that bind to the sterol regulatory element DNA sequence TCACNCCAC. Mammalian SREBPs are encoded by the genes SREBF1 and SREBF2. SREBPs belong to the basic-helix-loop-helix leucine zipper class of transcription factors. Unactivated SREBPs are attached to the nuclear envelope and endoplasmic reticulum membranes. In cells with low levels of sterols, SREBPs are cleaved to a water-soluble N-terminal domain that is translocated to the nucleus. These activated SREBPs then bind to specific sterol regulatory element DNA sequences, thus upregulating the synthesis of enzymes involved in sterol biosynthesis. Sterols in turn inhibit the cleavage of SREBPs and therefore synthesis of additional sterols is reduced through a negative feed back loop.

词汇	SREBP
分类	英语词汇英语翻译词典
释义	SREBP 英语百科 Sterol regulatory element-binding protein （重定向自SREBP） Sterol regulatory element-binding proteins (SREBPs) are transcription factors that bind to the sterol regulatory element DNA sequence TCACNCCAC. Mammalian SREBPs are encoded by the genes SREBF1 and SREBF2. SREBPs belong to the basic-helix-loop-helix leucine zipper class of transcription factors. Unactivated SREBPs are attached to the nuclear envelope and endoplasmic reticulum membranes. In cells with low levels of sterols, SREBPs are cleaved to a water-soluble N-terminal domain that is translocated to the nucleus. These activated SREBPs then bind to specific sterol regulatory element DNA sequences, thus upregulating the synthesis of enzymes involved in sterol biosynthesis. Sterols in turn inhibit the cleavage of SREBPs and therefore synthesis of additional sterols is reduced through a negative feed back loop.
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