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

ABC Transporters: Exporter01:31

ABC Transporters: Exporter

4.1K
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...
4.1K
Nuclear Export01:42

Nuclear Export

3.6K
The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
3.6K
Primary Active Transport01:47

Primary Active Transport

173.4K
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...
173.4K
Protein Import into the Peroxisomes01:27

Protein Import into the Peroxisomes

3.4K
Cells contain membrane-bound organelles called peroxisomes that oxidize organic molecules by transferring hydrogen atoms to oxygen, producing hydrogen peroxide. Peroxisomes enzymatically convert the released hydrogen peroxide into water and oxygen.
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
3.4K
Structure of Porins01:21

Structure of Porins

2.9K
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...
2.9K
Phosphorylation01:02

Phosphorylation

49.8K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
49.8K

You might also read

Related Articles

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

Sort by
Same author

The C9orf72/SMCR8 complex maintains microglial homeostasis via RAB8A-ESCRT-mediated lysosomal repair.

The EMBO journal·2026
Same author

The human plasma amino acids balance favours HIV replication in primary CD4 T lymphocytes.

bioRxiv : the preprint server for biology·2026
Same author

Molecular mechanism of phosphate import by the bacterial PstSCAB transporter.

Nature communications·2026
Same author

Author Correction: Mitochondria-associated condensates maintain mitochondrial homeostasis and promote lifespan.

Nature aging·2025
Same author

Mitochondria-associated condensates maintain mitochondrial homeostasis and promote lifespan.

Nature aging·2025
Same author

Gating mechanism of the two-pore-domain potassium channel THIK1.

Nature structural & molecular biology·2025

Related Experiment Video

Updated: Jun 2, 2025

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
08:49

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Published on: March 14, 2021

3.9K

Structural basis of phosphate export by human XPR1.

Qixian He1, Ran Zhang2, Sandrine Tury3

  • 1Center for Life Sciences, Yunnan Key Laboratory of Cell Metabolism and Diseases, State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan, School of Life Sciences, Yunnan University, Kunming, China.

Nature Communications
|January 15, 2025
PubMed
Summary

The study reveals the structure of human XPR1, a phosphate exporter crucial for cellular phosphate balance. Inositol pyrophosphate binding regulates XPR1

More Related Videos

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time
08:33

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time

Published on: March 11, 2021

1.9K
Analysis of Minerals Produced by hFOB 1.19 and Saos-2 Cells Using Transmission Electron Microscopy with Energy Dispersive X-ray Microanalysis
14:55

Analysis of Minerals Produced by hFOB 1.19 and Saos-2 Cells Using Transmission Electron Microscopy with Energy Dispersive X-ray Microanalysis

Published on: June 24, 2018

9.1K

Related Experiment Videos

Last Updated: Jun 2, 2025

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
08:49

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Published on: March 14, 2021

3.9K
Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time
08:33

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time

Published on: March 11, 2021

1.9K
Analysis of Minerals Produced by hFOB 1.19 and Saos-2 Cells Using Transmission Electron Microscopy with Energy Dispersive X-ray Microanalysis
14:55

Analysis of Minerals Produced by hFOB 1.19 and Saos-2 Cells Using Transmission Electron Microscopy with Energy Dispersive X-ray Microanalysis

Published on: June 24, 2018

9.1K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Biology

Background:

  • Cellular phosphate homeostasis is vital for all life.
  • XPR1 (inositol pyrophosphate-dependent phosphate exporter) plays a role in vertebrate phosphate regulation.
  • XPR1's precise mechanism and structure remain poorly understood.

Purpose of the Study:

  • To elucidate the three-dimensional structure of human XPR1 using cryo-electron microscopy (cryo-EM).
  • To identify the phosphate binding site and key residues involved in XPR1 function.
  • To understand how inositol pyrophosphate binding regulates XPR1 activity.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine the structure of human XPR1.
  • Structural analysis to identify domains, transmembrane helices, and ligand-binding sites.
  • Comparative structural analysis with related proteins (e.g., ion-translocating rhodopsins).

Main Results:

  • The cryo-EM structure of human XPR1 revealed a dimeric complex with 10 transmembrane helices per protomer.
  • A phosphate-binding site was identified within a core domain tunnel, featuring basic residues and a conserved W573.
  • Inositol pyrophosphate binding was linked to structural changes in TM9 and W573, affecting the extracellular vestibule and export function.

Conclusions:

  • The determined structure provides atomic-level insights into the XPR1 phosphate exporter mechanism.
  • A conserved tryptophan (W573) and associated structural rearrangements are critical for phosphate export.
  • This work lays the foundation for future research into XPR1 function and regulation in phosphate homeostasis.