Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Secondary Active Transport01:32

Secondary Active Transport

9.8K
One example of how cells use the energy contained in electrochemical gradients is demonstrated by glucose transport into cells. The ion vital to this process is sodium (Na+), which is typically present in higher concentrations extracellularly than in the cytosol. Such a concentration difference is due, in part, to the action of an enzyme "pump" embedded in the cellular membrane that actively expels Na+ from a cell. Importantly, as this pump contributes to the high concentration of...
9.8K
Secondary Active Transport01:55

Secondary Active Transport

138.5K
One example of how cells use the energy contained in electrochemical gradients is demonstrated by glucose transport into cells. The ion vital to this process is sodium (Na+), which is typically present in higher concentrations extracellularly than in the cytosol. Such a concentration difference is due, in part, to the action of an enzyme “pump” embedded in the cellular membrane that actively expels Na+ from a cell. Importantly, as this pump contributes to the high concentration of...
138.5K
Pore Transport and Ion-Pair Transport01:17

Pore Transport and Ion-Pair Transport

1.4K
Pore transport and ion-pair formation are critical mechanisms for the absorption and distribution of drugs in the body.
Pore transport, also known as convective transport, is a process where small molecules like urea, water, and sugars rapidly cross cell membranes as though there were channels or pores in the membrane. Although direct microscopic evidence is limited  but the concept of pores or channels is widely accepted based on physiological evidence. Despite the lack of direct...
1.4K
Primary Active Transport01:29

Primary Active Transport

14.7K
In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction they would...
14.7K
Primary Active Transport01:47

Primary Active Transport

201.4K
In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps that are embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction...
201.4K
The Significance of Membrane Transport01:44

The Significance of Membrane Transport

42.9K
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...
42.9K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Targeting Protein-Protein Interactions (PPIs) to Drive Functional Annotation: An Integrative Methodology to Study Senescence-Associated PPIs Using TMPRSS11a as Model Interactor.

Biomolecules·2026
Same author

Computational Mapping and Targeting of BK Channel Protein-Protein Interactions in Breast Cancer.

Journal of chemical information and modeling·2026
Same author

Identification of 14-3-3 Proteins as Binding Partners of TRP Channels.

Journal of chemical information and modeling·2026
Same author

ReaxFF Parameter Set for Boron Clusters and Icosahedral Boron Crystals: Comparison with Density Functional Theory and Machine-Learning Potentials.

The journal of physical chemistry. C, Nanomaterials and interfaces·2025
Same author

Exploring a peripheral PIP2-binding site and its role in the alternative regulation of the TRP channel superfamily.

The Journal of general physiology·2025
Same author

Growth of Hexagonal Boron Nitride from Molten Nickel Solutions: A Reactive Molecular Dynamics Study.

ACS applied materials & interfaces·2025

Related Experiment Video

Updated: Feb 18, 2026

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting
10:08

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting

Published on: December 9, 2022

2.6K

Iodide Binding in Sodium-Coupled Cotransporters.

Ariela Vergara-Jaque1,2, Peying Fong3, Jeffrey Comer2,3

  • 1Center for Bioinformatics and Molecular Simulation, Universidad de Talca , 2 Norte 685, Talca 3460000, Chile.

Journal of Chemical Information and Modeling
|November 14, 2017
PubMed
Summary
This summary is machine-generated.

Structural analysis reveals conserved iodide-binding pockets in thyroid transporters. Mutations in sodium-iodide symporter (NIS) and sodium-coupled monocarboxylate transporter 1 (SMCT1) impact iodide affinity, suggesting SMCT1

More Related Videos

Application of Electrophysiology Measurement to Study the Activity of Electro-Neutral Transporters
11:51

Application of Electrophysiology Measurement to Study the Activity of Electro-Neutral Transporters

Published on: February 3, 2018

7.5K
Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
12:48

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays

Published on: February 19, 2013

11.2K

Related Experiment Videos

Last Updated: Feb 18, 2026

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting
10:08

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting

Published on: December 9, 2022

2.6K
Application of Electrophysiology Measurement to Study the Activity of Electro-Neutral Transporters
11:51

Application of Electrophysiology Measurement to Study the Activity of Electro-Neutral Transporters

Published on: February 3, 2018

7.5K
Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
12:48

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays

Published on: February 19, 2013

11.2K

Area of Science:

  • Molecular biology
  • Biophysics
  • Cellular physiology

Background:

  • Apical iodide efflux from thyroid follicular cells involves proposed pathways, including the controversial sodium-coupled monocarboxylate transporter 1 (SMCT1).
  • The sodium-iodide symporter (NIS) mediates the initial iodide uptake into thyroid cells and is well-characterized.

Purpose of the Study:

  • To evaluate structural and functional similarities between SMCT1 and NIS.
  • To investigate the role of specific residues in iodide binding and transport.

Main Methods:

  • Free-energy calculations using a force field with electronic polarizability.
  • Site-directed mutagenesis of human NIS (hNIS) and human SMCT1 (hSMCT1) residues.
  • Assessment of iodide binding affinity and transport function.

Main Results:

  • A conserved iodide-binding pocket was identified in hNIS, involving TM2, TM3, and TM7 segments and coordinating residues Phe67, Gln72, Cys91, and Gln94.
  • Mutation of Gly93 in hNIS to a larger amino acid altered the binding pocket and reduced iodide affinity, consistent with hypothyroidism.
  • The position of Trp255 in the hNIS mutant mirrored Trp253 in wild-type hSMCT1, and mutating Thr91 to Gly in hSMCT1 increased its iodide affinity, making its pocket resemble wild-type hNIS.

Conclusions:

  • Structural similarities exist between the iodide-binding sites of NIS and SMCT1.
  • Specific amino acid residues play critical roles in determining iodide affinity and transporter function.
  • Wild-type hSMCT1 may exhibit weak iodide binding in its inward-facing conformation, impacting its transport capabilities.