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Related Concept Videos

Nuclear Export01:42

Nuclear Export

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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...
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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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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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Directionality of Nuclear Transport01:42

Directionality of Nuclear Transport

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Ras-related nuclear protein or Ran is a small G protein that cycles between its GTP and GDP bound states. Ran specific regulators, a Ran GTPase Activating Protein or RanGAP present in the cytosol and a Ran guanine nucleotide exchange factor or RanGEF present inside the nucleus regulate GTP/GDP exchange. A high concentration of GTP inside the cells, in addition to this asymmetric distribution of  Ran-specific regulators, leads to a higher RanGTP concentration inside the nucleus. This...
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Primary Active Transport01:29

Primary Active Transport

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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...
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ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

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The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
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Related Experiment Video

Updated: May 20, 2025

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

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Structure and function of human XPR1 in phosphate export.

Long Chen1,2, Jin He1,2, Mingxing Wang3,4

  • 1MOE Key Laboratory for Cellular Dynamics, Hefei National Research Center for Interdisciplinary Sciences at the Microscale, Center for Advanced Interdisciplinary Science and Biomedicine of IHM, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China.

Nature Communications
|March 27, 2025
PubMed
Summary
This summary is machine-generated.

The structure of human XPR1, a phosphate exporter crucial for homeostasis and linked to brain calcification, was determined. This reveals key phosphate binding sites and conformational changes, explaining its transport mechanism.

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Last Updated: May 20, 2025

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Area of Science:

  • Structural Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Xenotropic and polytropic retrovirus receptor 1 (XPR1) is a phosphate exporter vital for human phosphate homeostasis.
  • XPR1 is implicated as a causative gene in primary familial brain calcification.
  • Understanding XPR1's structure is essential for elucidating its function and associated diseases.

Purpose of the Study:

  • To determine the cryogenic electron microscopy (cryo-EM) structure of human XPR1 (HsXPR1).
  • To elucidate the structural basis of XPR1-mediated phosphate transport.
  • To identify key residues and conformational states involved in XPR1 function.

Main Methods:

  • Cryogenic electron microscopy (cryo-EM) was used to determine the structure of human XPR1.
  • Analysis of the dimeric structure, transmembrane domain, core and scaffold domains.
  • Identification of phosphate-binding sites and investigation of mutations' effects on transport activity.

Main Results:

  • The cryo-EM structure of dimeric HsXPR1 was resolved, revealing its architecture.
  • Two critical phosphate-binding sites within the pore-like core domain were identified, with mutations impairing transport.
  • A new V-shaped conformation of the cytoplasmic SPX domains was observed, suggesting dynamic functional states.

Conclusions:

  • The study provides the structural basis for XPR1-mediated phosphate export.
  • Key structural features and residues essential for HsXPR1 transport activity were elucidated.
  • These findings offer insights into the molecular mechanisms underlying phosphate homeostasis and primary familial brain calcification.