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Sterol is an organic compound [1] with formula C 17 H 28 O , whose molecule is derived from that of gonane by replacement of a hydrogen atom on C3 position by a hydroxyl group.
Proteolytic cleavage frees it to move through the cytoplasm to the nucleus. Once in the nucleus, SREBP can bind to specific DNA sequences (the sterol regulatory elements or SREs) that are found in the control regions of the genes that encode enzymes needed to make lipids. This binding to DNA leads to the increased transcription of the target genes.
Sterol carrier proteins (also known as nonspecific lipid transfer proteins) is a family of proteins that transfer steroids and probably also phospholipids and gangliosides between cellular membranes. These proteins are different from plant nonspecific lipid transfer proteins but structurally similar to small proteins of unknown function from ...
All known sterols in eukaryotes are enzymatically extensively modified from protosterols, while organisms that only produce protosterols are not known. The oldest record of modified steranes are in sedimentary rocks deposited ca. 720–820 million years ago. [ 5 ]
SCAP is a regulatory protein that is required for the proteolytic cleavage of the sterol regulatory element-binding protein . SCAP is an integral membrane protein located in the endoplasmic reticulum (ER). One of the cytosolic regions of SCAP contains a hexapeptide amino acid sequence, MELADL, that functions to detect cellular cholesterol. When ...
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You are free: to share – to copy, distribute and transmit the work; to remix – to adapt the work; Under the following conditions: attribution – You must give appropriate credit, provide a link to the license, and indicate if changes were made.
Sterol regulatory element-binding transcription factor 1 (SREBF1) also known as sterol regulatory element-binding protein 1 (SREBP-1) is a protein that in humans is encoded by the SREBF1 gene. [5] [6] This gene is located within the Smith–Magenis syndrome region on chromosome 17.