Steroidogenic acute regulatory protein (StAR) retains activity in the absence of its mitochondrial import sequence: Implications for the mechanism of StAR action
Open accessAbstract
Steroidogenic acute regulatory protein (StAR) plays a critical role in steroid hormone biosynthesis, presumably by facilitating the delivery of cholesterol to P450scc in the inner mitochondrial membranes. StAR is synthesized as a 37-kDa preprotein that is processed to a 30-kDa mature form by cleavage of an N-terminal mitochondrial import sequence. To identify structural features required for StAR biological activity, we mutated the human StAR cDNA, including the deletion of N- and C-terminal sequences, and examined the ability of the mutants to promote steroidogenesis and enter the mitochondria of transfected COS-1 cells. Deletion of up to 62 residues from the N terminus (N-62) did not significantly affect steroidogenesis-enhancing activity. The N-terminal deletion mutants were associated with mitochondria-enriched fractions, but import and processing were progressively impaired with increasing length of the deletion. Immunogold electron microscopy and in vitro import assays showed that the active N-62 mutant was not imported into the mitochondria. Removal of the 28 C-terminal amino acids (C-28) inactivated StAR. Deletion of the C-terminal 10 amino acids (C-10) reduced steroidogenic activity by 53%, while truncation of the last 4 amino acids had no effect. The C-28 mutant StAR was not efficiently imported into mitochondria or processed, whereas some of the C-10 mutant was processed, indicating that import had occurred. We conclude that in the COS-1 cell system used, StAR does not need to enter into mitochondria to stimulate steroidogenesis and that residues in the C terminus are essential for steroidogenesis-enhancing activity. These findings imply that StAR acts via C-terminal domains on the outside of the mitochondria.
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When expressed in cytoplasm or added to mitochondria in vitro, both the 37- and 30-kDa forms of StAR are equally active.
“When expressed in cytoplasm or added to mitochondria in vitro, both the 37-and 30-kDa forms of StAR are equally active (77).”
From The Molecular Biology, Biochemistry, and Physiology of Human Steroidogenesis and Its Disorders (2011) · cites this paper as [77]
The Results and Discussion (page not provided) report that N-terminally truncated StAR retained steroidogenic activity comparable to wild-type StAR in transfected COS-1 cells, even though the N-62 mutant was not imported into mitochondria. The paper says N-62 migrated at approximately the same molecular weight as mature StAR, but it does not establish equal activity of the 37- and 30-kDa forms when added to mitochondria in vitro; its in vitro assay tested import and processing, not steroidogenic activity. (LLM, conf=0.87)
Experimental — accuracy not yet measuredStAR acts exclusively on the OMM, and its activity in promoting steroidogenesis is proportional to its residency time on the OMM.
“These data demonstrate that StAR acts exclusively on the OMM (77, 78), and its activity in promoting steroidogenesis is proportional to its residency time on the OMM (78).”
From The Molecular Biology, Biochemistry, and Physiology of Human Steroidogenesis and Its Disorders (2011) · cites this paper as [77]
The Results and Discussion conclude from COS-1 cell experiments that StAR can stimulate steroidogenesis without entering mitochondria, which supports action at or outside the outer mitochondrial membrane. The Implications for the Mechanism of StAR Action section (p. 13735) calls outer-membrane action presumptive and continuous action while associated with that membrane hypothetical; it does not establish exclusive action or show that activity is proportional to residence time. (LLM, conf=0.88)
Experimental — accuracy not yet measuredDeletion of the first 62 amino-terminal residues has no effect on StAR activity assayed in vitro, although it deletes the entire mitochondrial leader sequence and forces StAR to remain in the cytoplasm.
“By contrast, deletion of the first 62 amino-terminal residues has no effect on StAR activity assayed in vitro, although this deletes the entire mitochondrial leader sequence and forces StAR to remain in the cytoplasm (77).”
From The Molecular Biology, Biochemistry, and Physiology of Human Steroidogenesis and Its Disorders (2011) · cites this paper as [77]
The Results and Discussion report that deleting the first 62 residues left steroidogenesis-enhancing activity unimpaired in transfected COS-1 cells and prevented mitochondrial import. However, activity was measured in cells, not in an in vitro activity assay; the in vitro assay tested import. The same section locates the N-62 mutant primarily on the outer mitochondrial membrane, rather than confined to the cytoplasm (page not supplied). (LLM, conf=0.90)
Experimental — accuracy not yet measuredStAR stimulates steroid production in cell model systems without its leader sequence and import into mitochondria.
“Surprisingly, StAR was found to stimulate steroid production in cell model systems without its leader sequence and import into the mitochondria (138).”
From Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies (2016) · cites this paper as [138]
Deletion of only 10 carboxy-terminal residues reduces StAR activity by half.
“Deletion of only 10 carboxy-terminal residues reduces StAR activity by half (77),”
From The Molecular Biology, Biochemistry, and Physiology of Human Steroidogenesis and Its Disorders (2011) · cites this paper as [77]
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- Authors
- Arakane, F., Sugawara, T., Nishino, H., Liu, Z., Holt, J. A., Pain, D., Stocco, D. M., Miller, W. L., & Strauss, J. F.
- Affiliations
- Texas Tech University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1996-11-26
- Volume
- 93
- Issue
- 24
- Pages
- 13731-13736
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC19407
- OpenAlex
- W2053497150
- Cited by
- 304
- References
- 21
- Citations by year
- 2026: 2 · 2025: 10 · 2024: 5 · 2023: 6 · 2022: 5 · 2021: 4 · 2020: 4 · 2019: 1 · 2018: 5 · 2017: 9 · 2016: 20 · 2015: 5 · 2014: 11 · 2013: 12 · 2012: 11
- FWCI
- 5.94
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- University of Pennsylvania
- Lalor Foundation
- National Institutes of Health (HD06274, DK 19525, HD17481)
- U.S. Public Health Service
- National Institute of Diabetes and Digestive and Kidney Diseases (DK 19525, P30DK019525)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD-06274, R01HD017481, P01HD006274, HD17481, R37HD017481)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Steroid Chemistry and Biochemistry
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adrenal Hormones and Disorders
- Keywords
- steroidogenic acute regulatory protein, stars, steroidogenesis, cholesterol transport, mitochondrial protein import, C-terminal domain, N-terminal deletion mutants, P450scc, protein processing
- MeSH terms
- Steroidogenic Acute Regulatory Protein, Animals, Humans, Mitochondria, Phosphoproteins, Recombinant Proteins, Transfection, Microscopy, Immunoelectron, Mutagenesis, Site-Directed, Sequence Deletion, DNA, Complementary, COS Cells, Mice
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