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Related Concept Videos

Aquaporins01:25

Aquaporins

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Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.
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ATP Driven Pumps III: V-type Pumps01:30

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V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
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ATP Driven Pumps I: An Overview01:27

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ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
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Reabsorption and Secretion in the DCT and Collecting Duct01:26

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The early phase of the DCT manages the reabsorption of approximately 10-15% of filtered water, 5–10% of filtered sodium, and 5–10% of filtered chloride. This process is facilitated by Na+–Cl− symporters in apical membranes and sodium-potassium pumps, as well as Cl− leakage channels in basolateral membranes. The early DCT also stands out as a site where parathyroid hormone (PTH) stimulates calcium reabsorption, depending on the body's requirements.
The distal...
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Prokaryotic Cells01:51

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Prokaryotes are small unicellular organisms that include the domains—Archaea and Bacteria. Bacteria include many common organisms, such as Salmonella and E. coli, while the Archaea include extremophiles that live in harsh environments, such as volcanic springs.
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Prokaryotic Cells01:28

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Prokaryotes are small unicellular organisms that include the domains — Archaea and Bacteria. Bacteria include many common microorganisms, such as Salmonella and E. coli, while the Archaea include extremophiles that live in harsh environments, such as volcanic springs.
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Measuring the Osmotic Water Permeability Coefficient Pf of Spherical Cells: Isolated Plant Protoplasts as an Example
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Prokaryotic Aquaporins.

Huichun Tong1,2, Qingqing Hu3,4, Lin Zhu5,6

  • 1State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, No.1 Beichen West Road, Chaoyang District, Beijing 100101, China. tonghuichun@im.ac.cn.

Cells
|October 27, 2019
PubMed
Summary
This summary is machine-generated.

Prokaryotic aquaporins, integral membrane proteins, are widespread but poorly understood. This study characterized their distribution and function, revealing diverse roles beyond water transport and suggesting novel regulatory mechanisms.

Keywords:
aquaporinsfacilitated diffusionhydrogen peroxideprokaryoteselective filtertetramer

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Area of Science:

  • Membrane Biology
  • Microbial Genomics
  • Protein Science

Background:

  • Aquaporins are vital membrane proteins facilitating transport in diverse organisms.
  • Prokaryotic aquaporins are less understood, despite their ubiquity.
  • Existing knowledge primarily focuses on model organisms like Escherichia coli.

Purpose of the Study:

  • To investigate the distribution and sequence characteristics of prokaryotic aquaporins.
  • To summarize their transport functions, physiological roles, and regulation.
  • To highlight novel findings and propose future research directions.

Main Methods:

  • Bioinformatic analysis of prokaryotic genomes from the KEGG database.
  • Sequence characterization focusing on the aromatic/arginine constriction region.
  • Literature review of known prokaryotic aquaporin functions and regulations.

Main Results:

  • Aquaporin homologues identified in 3315 prokaryotic genomes.
  • Protein clustering did not fully align with species phylogeny.
  • Diversified amino acid compositions in the ar/R region suggest varied functions.
  • A Streptococcus aquaporin demonstrated hydrogen peroxide efflux, aiding detoxification and competitiveness.
  • Novel post-translational regulatory mechanisms were identified.

Conclusions:

  • Prokaryotic aquaporins exhibit significant diversity in sequence and function.
  • Their roles extend beyond simple water transport, including detoxification and inter-species interactions.
  • Further research is crucial to fully elucidate the functional repertoire and working mechanisms of these proteins.