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Abstract
The 17β-hydroxysteroid dehydrogenases (17β-HSDs) comprise enzymes initially identified
by their ability to interconvert active and inactive forms of sex steroids, a vital
process for the tissue-specific control of estrogen and androgen balance. However,
most 17β-HSDs have now been shown to accept substrates other than sex steroids, including
bile acids, retinoids and fatty acids, thereby playing unanticipated roles in cell
physiology. This functional divergence is often reflected by their different subcellular
localization, with 17β-HSDs found in the cytosol, peroxisome, mitochondria, endoplasmic
reticulum and in lipid droplets. Moreover, a subset of 17β-HSDs are integral membrane
proteins, with their specific topology dictating the cellular compartment in which
they exert their enzymatic activity. Here, we summarize the present knowledge on the
subcellular localization and membrane topology of the 17β-HSD enzymes and discuss
the correlation with their biological functions.