ArticleThe Journal of biological chemistry2015
Heterodimerization, altered subcellular localization, and function of multiple zinc transporters in viable cells using bimolecular fluorescence complementation.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 46 citations in OpenAlex.
- Subcellular localization as a driver of protein function.Nature reviews. Molecular cell biology · 2026Review
- Lysosome-related organelles employ divergent mechanisms to modulate cytosolic zinc homeostasis.PLoS genetics · 2026Article
- Comprehensive characterization of poplar HSP20 gene family: genome-wide identification, stress-induced expression profiling, and protein interaction verifications.BMC plant biology · 2025Article
- The zinc transporter Slc30a1 (ZnT1) in macrophages plays a protective role against attenuatedeLife · 2024Article
- Localization of the MTP4 transporter to trans-Golgi network in pollen tubes of Arabidopsis thaliana.Journal of plant research · 2024Article
- Pigmentation and TYRP1 expression are mediated by zinc through the early secretory pathway-resident ZNT proteins.Communications biology · 2023Article
- Transmembrane 163 (TMEM163) protein interacts with specific mammalian SLC30 zinc efflux transporter family members.Biochemistry and biophysics reports · 2022Article
- Lysosomal inhibition sensitizes TMEM16A-expressing cancer cells to chemotherapy.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Zinc Signaling in the Mammary Gland: For Better and for Worse.Biomedicines · 2021Review
- The Multifaceted Roles of Zinc in Neuronal Mitochondrial Dysfunction.Biomedicines · 2021Review
- Transmembrane 163 (TMEM163) Protein: A New Member of the Zinc Efflux Transporter Family.Biomedicines · 2021Review
- Frontline Science: LPS-inducible SLC30A1 drives human macrophage-mediated zinc toxicity against intracellular Escherichia coli.Journal of leukocyte biology · 2021Article
- Transcription factors and transporters in zinc homeostasis: lessons learned from fungi.Critical reviews in biochemistry and molecular biology · 2020Review
- Transmembrane 163 (TMEM163) protein effluxes zinc.Archives of biochemistry and biophysics · 2019Article
- Milk-derived miRNA profiles elucidate molecular pathways that underlie breast dysfunction in women with common genetic variants in SLC30A2.Scientific reports · 2019Article
- Alterations in ZnT1 expression and function lead to impaired intracellular zinc homeostasis in cancer.Cell death discovery · 2019Article
- Demonstrating aspects of multiscale modeling by studying the permeation pathway of the human ZnT2 zinc transporter.PLoS computational biology · 2018Article
- Evaluation of the roles of the cytosolic N-terminus and His-rich loop of ZNT proteins using ZNT2 and ZNT3 chimeric mutants.Scientific reports · 2018Article
- NADPH Oxidases and Mitochondria in Vascular Senescence.International journal of molecular sciences · 2018Review
- Understanding the Contribution of Zinc Transporters in the Function of the Early Secretory Pathway.International journal of molecular sciences · 2017Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Zinc plays a crucial role in numerous key physiological functions. Zinc transporters (ZnTs) mediate zinc efflux and compartmentalization in intracellular organelles; thus, ZnTs play a central role in zinc homeostasis. We have recently shown the in situ dimerization and function of multiple normal and mutant ZnTs using bimolecular fluorescence complementation (BiFC). Prompted by these findings, we here uncovered the heterodimerization, altered subcellular localization, and function of multiple ZnTs in live cells using this sensitive BiFC technique. We show that ZnT1, -2, -3, and -4 form stable heterodimers at distinct intracellular compartments, some of which are completely different from their homodimer localization. Specifically, unlike the plasma membrane (PM) localization of ZnT1 homodimers, ZnT1-ZnT3 heterodimers localized at intracellular vesicles. Furthermore, upon heterodimerization with ZnT1, the zinc transporters ZnT2 and ZnT4 surprisingly localized at the PM, as opposed to their vesicular homodimer localization. We further demonstrate the deleterious effect that the G87R-ZnT2 mutation, associated with transient neonatal zinc deficiency, has on ZnT1, ZnT3, and ZnT4 upon heterodimerization. The functionality of the various ZnTs was assessed by the dual BiFC-Zinquin assay. We also undertook a novel transfection competition assay with ZnT cDNAs to confirm that the driving force for heterodimer formation is the core structure of ZnTs and not the BiFC tags. These findings uncover a novel network of homo- and heterodimers of ZnTs with distinct subcellular localizations and function, hence highlighting their possible role in zinc homeostasis under physiological and pathological conditions.
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