ArticleMolecular and cellular biology2001
Dimerization of sterol regulatory element-binding protein 2 via the helix-loop-helix-leucine zipper domain is a prerequisite for its nuclear localization mediated by importin beta.
Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 70 citations in OpenAlex.
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- Metabolic Injury of Hepatocytes Promotes Progression of NAFLD and AALD.Seminars in liver disease · 2022Review
- Cholesterol Metabolic Reprogramming in Cancer and Its Pharmacological Modulation as Therapeutic Strategy.Frontiers in oncology · 2021Review
- Identification of a degradation signal at the carboxy terminus of SREBP2: A new role for this domain in cholesterol homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Mechanism of self/nonself-discrimination in Brassica self-incompatibility.Nature communications · 2020Article
- SREBP-regulated lipid metabolism: convergent physiology - divergent pathophysiology.Nature reviews. Endocrinology · 2017Review
- A genome-wide interactome of DNA-associated proteins in the human liver.Genome research · 2017Article
- Enriching Traditional Protein-protein Interaction Networks with Alternative Conformations of Proteins.Scientific reports · 2017Article
- Post-translational regulation of rice MADS29 function: homodimerization or binary interactions with other seed-expressed MADS proteins modulate its translocation into the nucleus.Journal of experimental botany · 2014Article
- Protein phosphatase 2A (PP2A) regulates low density lipoprotein uptake through regulating sterol response element-binding protein-2 (SREBP-2) DNA binding.The Journal of biological chemistry · 2014Article
- G proteins, p60TRP, and neurodegenerative diseases.Molecular neurobiology · 2013Review
- Nuclear transport modulation reduces hypercholesterolemia, atherosclerosis, and fatty liver.Journal of the American Heart Association · 2013Article
- Nonmyofilament-associated troponin T3 nuclear and nucleolar localization sequence and leucine zipper domain mediate muscle cell apoptosis.Cytoskeleton (Hoboken, N.J.) · 2013Article
- Article
- Nuclear-cytoplasmic shuttling of Chibby controls beta-catenin signaling.Molecular biology of the cell · 2010Article
- Mechanisms and signals for the nuclear import of proteins.Current genomics · 2009Article
- Evolutionary conservation and adaptation in the mechanism that regulates SREBP action: what a long, strange tRIP it's been.Genes & development · 2009Review
- In vitro nuclear interactome of the HIV-1 Tat protein.Retrovirology · 2009Article
- Chibby forms a homodimer through a heptad repeat of leucine residues in its C-terminal coiled-coil motif.BMC molecular biology · 2009Article
- Effect of Daxx on cholesterol accumulation in hepatic cells.World journal of gastroenterology · 2008Article
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
The sterol regulatory element-binding protein 2 (SREBP-2), a transcription factor of the basic helix-loop-helix-leucine zipper (bHLH-Zip) family, is synthesized in the form of a membrane-attached precursor molecule. When cells are deprived of sterols, a two-step proteolytic processing releases the transcriptionally active N-terminal segment of SREBP-2, thereby allowing it to enter the nucleus. In previous studies, we showed that the nuclear import of SREBP-2 occurs via the direct interaction of importin beta with the HLH-Zip domain. In this study, in order to more completely understand the intracellular dynamics of SREBP-2, we focused on the manner by which importin beta recognizes SREBP-2 at the initial step of the import. It was found that the active form of SREBP-2 exists as a stable dimer in solution and that the substitution of leucine residues for alanine in the leucine zipper motif disrupted the dimerization. It was also demonstrated that this mutant protein did not enter the nucleus either in vivo or in vitro. Solution binding assays, which involved the chemical cross-linking of wild-type or mutated SREBP-2 with importin beta, revealed that the import-active complex appeared to be composed of a dimeric form of SREBP-2 and importin beta. In addition, the SREBP-2 binding domain of importin beta corresponded to an overlapping but not identical region for importin alpha binding, which may explain how importin beta is able to recognize the dimeric HLH-Zip directly. These results indicate that dimerization is a prerequisite process for the nuclear import of SREBP-2 mediated by importin beta.
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