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The ADP/ATP Carrier Protein01:42

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ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
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Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
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Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
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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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Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time
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NAADP-Dependent TPC Current.

Qiaochu Wang1,2, Michael X Zhu3

  • 1Beijing Children's Hospital, Capital Medical University, Beijing, China.

Handbook of Experimental Pharmacology
|July 28, 2022
PubMed
Summary
This summary is machine-generated.

Two-pore channels (TPCs) are vital for cellular processes. This study investigates how PI(3,5)P2 and NAADP regulate TPCs, suggesting dual, interdependent control of these critical ion channels.

Keywords:
AutophagyCa2+ signalingEndolysosome patch clampLysosome channelsTPC1TPC2

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Area of Science:

  • Cellular Biology
  • Ion Channel Physiology
  • Molecular Signaling

Background:

  • Two-pore channels (TPCs), TPC1 and TPC2, are Ca2+ and Na+-permeable cation channels found on endosome and lysosome membranes in mammalian cells.
  • TPCs are involved in diverse cellular functions including Ca2+ signaling, vesicular trafficking, metabolism, macropinocytosis, and viral infection.
  • While TPCs mediate Ca2+ release from acidic organelles in response to nicotinic acid adenine dinucleotide phosphate (NAADP), their direct ligand interaction remains debated.

Purpose of the Study:

  • To investigate the regulation of TPCs by PI(3,5)P2 and NAADP.
  • To explore the relationship between NAADP-elicited TPC2 currents and PI(3,5)P2-evoked currents.
  • To propose a model for the dual and interdependent regulation of TPCs by these endogenous ligands.

Main Methods:

  • Whole-endolysosomal patch clamp recordings were utilized to study ion channel activity.
  • Experiments focused on detecting NAADP-evoked currents in vacuoles expressing TPC1 or TPC2.
  • Analysis of PI(3,5)P2-activated currents under similar experimental conditions.

Main Results:

  • Direct NAADP-evoked currents were difficult to detect in TPC1/TPC2 expressing vacuoles using whole-endolysosomal patch clamp.
  • Phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) activated a highly Na+-selective current under the same conditions.
  • Observations suggest NAADP can elicit TPC2 currents from enlarged endolysosomes, with potential links to PI(3,5)P2-evoked currents.

Conclusions:

  • TPCs are likely dually regulated by both PI(3,5)P2 and NAADP in an interdependent manner.
  • These two endogenous ligands may exert both distinct and cooperative roles in TPC channel function.
  • Further research is warranted to fully elucidate the complex regulatory mechanisms of TPCs.