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Related Concept Videos

The Significance of Membrane Transport01:44

The Significance of Membrane Transport

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The transport of solutes across the cell membrane is essential for metabolic processes, like maintaining cell size and volume, generating the action potential, exchanging nutrients and gases, etc. Membrane transport can be either passive or active. It can be simple diffusion, facilitated, or mediated transport aided by transport proteins such as transporters and channels.
Transporters facilitate either an active or passive movement of solutes. They can allow a single-molecule transport down its...
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ABC Transporters: Exporter01:31

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ATP-binding cassette or ABC transporter is the largest superfamily of integral membrane proteins. The transporters have transmembrane-binding domains (TMDs) and nucleotide-binding domains (NBDs). The TMDs are specific to their substrates, whereas the NBDs are similar to engines that complete ATP hydrolysis to complete the substrate transport. They can be full transporters consisting of two TMDs and NBDs, half transporters with one TMD and NBD, while some encoded with a single TMD or NBD are...
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ABC Transporters: Importer01:27

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ATP-binding cassette or ABC transporters are a class of ATP-driven pumps that hydrolyze ATP to move solutes across the membrane. They can be grouped into importers and exporters. While exporters are present in all domains of life, importers exist only in bacteria and some plants.
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Facilitated Diffusion01:16

Facilitated Diffusion

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The plasma membrane, a critical structure in cellular biology, houses an array of transporters, or carrier proteins, interspersed within its lipid bilayer. These proteins play a crucial role in solute transport through facilitated diffusion, a form of passive diffusion that uses transporters to move the molecules across the membrane.
In this process, substrates such as organic compounds and ions interact with a transporter on one side, triggering conformational changes in proteins that enable...
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Membrane Transporters01:31

Membrane Transporters

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Transporters are essential membrane transport proteins with functions related to cell nutrition, homeostasis, communication, etc. Approximately 7% of all genes in the human genome code for transporters or transporter-related proteins.
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Structure of Porins01:21

Structure of Porins

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Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
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Related Experiment Video

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Author Spotlight: Exploring Cellular Zinc Regulation Through ZnT1 Functionality
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A homology-based 3D model and structure-function studies reveal key elements for divalent metal ion transporter ZIP8

Sven P Baumann1, Gergely Gyimesi2, Giuseppe Albano2

  • 1Department of Nephrology and Hypertension, Inselspital, University of Bern, Bern, Switzerland; Department of Biomedical Research, Inselspital, University of Bern, Bern, Switzerland; Graduate School for Cellular and Biomedical Sciences, University of Bern, Bern, Switzerland.

The Journal of Biological Chemistry
|November 13, 2025
PubMed
Summary

The divalent metal transporter ZIP8 (SLC39A8) is crucial for nutrient homeostasis. Researchers modeled ZIP8, identifying key metal-binding sites (M1, M2, M4) essential for manganese, zinc, and iron transport, revealing insights into disease associations.

Keywords:
SLCSLC39A8ZIP8bicarbonatecotransporthomology-based 3D modelironmanganesemembrane transportmetal ion homeostasismutagenesissolute carrier proteinstructure–function studieszinc

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A Proteoliposome-Based Efflux Assay to Determine Single-molecule Properties of Cl- Channels and Transporters
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Essential Metal Uptake in Gram-negative Bacteria: X-ray Fluorescence, Radioisotopes, and Cell Fractionation
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • The divalent metal transporter ZIP8 (Zrt/Irt-like protein 8; SLC39A8) is vital for cellular homeostasis of essential metals like manganese, zinc, and iron.
  • Genetic variations in SLC39A8 are linked to various human diseases, including neuropsychiatric disorders, Crohn's disease, and obesity, highlighting its clinical significance.

Purpose of the Study:

  • To elucidate the structural basis of ZIP8-mediated metal transport by generating a homology-based 3D model.
  • To identify and characterize the amino acid residues and metal-binding sites involved in ZIP8 function.
  • To investigate the role of specific metal-binding sites in substrate selectivity and transport rates.

Main Methods:

  • Homology modeling to create a 3D structure of ZIP8.
  • Site-directed mutagenesis to alter specific amino acid residues within putative metal-binding sites.
  • Functional assays to assess metal transport activity, substrate selectivity, and transport rates.

Main Results:

  • Identification of three metal-binding sites (M1, M2, M4) within ZIP8, with M2 being essential for function and M1 contributing to substrate selectivity and transport efficiency.
  • Mutagenesis studies revealed specific residues critical for Fe2+ and Mn2+ transport and identified H347 as influencing turnover rates.
  • Direct evidence for Zn2+-HCO3- cotransport by human ZIP8 was established, along with insights into bicarbonate's modulatory role.

Conclusions:

  • The study provides a structural and functional framework for ZIP8 metal transport, detailing the roles of M1, M2, and M4 binding sites.
  • Findings offer new perspectives on how ZIP8 genetic variants may lead to disease and suggest potential therapeutic targets.
  • The discovery of Zn2+-HCO3- cotransport and bicarbonate's influence expands the understanding of ZIP8 regulation.