Steroid hormone synthesis begins with the conversion of cholesterol into pregnenolone by the enzyme cytochrome P450scc in mitochondria. The cholesterol used to synthesize pregnenolone is derived mainly from endocytosed LDL cholesterol. How this LDL cholesterol is transported to mitochondria in the human placenta is not well understood. Recent work has focused on how STARD3/MLN64 controls cholesterol trafficking. The STARD3 protein has a START domain that associates with cholesterol. Why STARD3 is distributed mainly to late endosomes but not to mitochondria is an obstacle to understanding the early steps in steroidogenesis. STARD3 can bind the ER protein VAP and contribute to ER-late endosome MCS formation. In this review, recent progress on STARD3 functions suggests possible models to explain how cholesterol could transit to mitochondria via MCS.
| Published in |
American Journal of Life Sciences (Volume 3, Issue 3-2)
This article belongs to the Special Issue Biology and Medicine of Peptide and Steroid Hormones |
| DOI | 10.11648/j.ajls.s.2015030302.19 |
| Page(s) | 48-52 |
| Creative Commons |
This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
| Copyright |
Copyright © The Author(s), 2015. Published by Science Publishing Group |
STARD3, steroidogenesis, endosome, mitochondria, cholesterol, membrane contact site
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APA Style
Atsuki Nara, Tohru Komiya. (2015). STARD3/MLN64 is Striving at Membrane Contact Sites: Intracellular Cholesterol Trafficking for Steroidogenesis in Human Placental Cells. American Journal of Life Sciences, 3(3-2), 48-52. https://doi.org/10.11648/j.ajls.s.2015030302.19
ACS Style
Atsuki Nara; Tohru Komiya. STARD3/MLN64 is Striving at Membrane Contact Sites: Intracellular Cholesterol Trafficking for Steroidogenesis in Human Placental Cells. Am. J. Life Sci. 2015, 3(3-2), 48-52. doi: 10.11648/j.ajls.s.2015030302.19
AMA Style
Atsuki Nara, Tohru Komiya. STARD3/MLN64 is Striving at Membrane Contact Sites: Intracellular Cholesterol Trafficking for Steroidogenesis in Human Placental Cells. Am J Life Sci. 2015;3(3-2):48-52. doi: 10.11648/j.ajls.s.2015030302.19
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Download@article{10.11648/j.ajls.s.2015030302.19,
author = {Atsuki Nara and Tohru Komiya},
title = {STARD3/MLN64 is Striving at Membrane Contact Sites: Intracellular Cholesterol Trafficking for Steroidogenesis in Human Placental Cells},
journal = {American Journal of Life Sciences},
volume = {3},
number = {3-2},
pages = {48-52},
doi = {10.11648/j.ajls.s.2015030302.19},
url = {https://doi.org/10.11648/j.ajls.s.2015030302.19},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajls.s.2015030302.19},
abstract = {Steroid hormone synthesis begins with the conversion of cholesterol into pregnenolone by the enzyme cytochrome P450scc in mitochondria. The cholesterol used to synthesize pregnenolone is derived mainly from endocytosed LDL cholesterol. How this LDL cholesterol is transported to mitochondria in the human placenta is not well understood. Recent work has focused on how STARD3/MLN64 controls cholesterol trafficking. The STARD3 protein has a START domain that associates with cholesterol. Why STARD3 is distributed mainly to late endosomes but not to mitochondria is an obstacle to understanding the early steps in steroidogenesis. STARD3 can bind the ER protein VAP and contribute to ER-late endosome MCS formation. In this review, recent progress on STARD3 functions suggests possible models to explain how cholesterol could transit to mitochondria via MCS.},
year = {2015}
}
TY - JOUR T1 - STARD3/MLN64 is Striving at Membrane Contact Sites: Intracellular Cholesterol Trafficking for Steroidogenesis in Human Placental Cells AU - Atsuki Nara AU - Tohru Komiya Y1 - 2015/05/06 PY - 2015 N1 - https://doi.org/10.11648/j.ajls.s.2015030302.19 DO - 10.11648/j.ajls.s.2015030302.19 T2 - American Journal of Life Sciences JF - American Journal of Life Sciences JO - American Journal of Life Sciences SP - 48 EP - 52 PB - Science Publishing Group SN - 2328-5737 UR - https://doi.org/10.11648/j.ajls.s.2015030302.19 AB - Steroid hormone synthesis begins with the conversion of cholesterol into pregnenolone by the enzyme cytochrome P450scc in mitochondria. The cholesterol used to synthesize pregnenolone is derived mainly from endocytosed LDL cholesterol. How this LDL cholesterol is transported to mitochondria in the human placenta is not well understood. Recent work has focused on how STARD3/MLN64 controls cholesterol trafficking. The STARD3 protein has a START domain that associates with cholesterol. Why STARD3 is distributed mainly to late endosomes but not to mitochondria is an obstacle to understanding the early steps in steroidogenesis. STARD3 can bind the ER protein VAP and contribute to ER-late endosome MCS formation. In this review, recent progress on STARD3 functions suggests possible models to explain how cholesterol could transit to mitochondria via MCS. VL - 3 IS - 3-2 ER -
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