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Related Concept Videos

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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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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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Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
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Related Experiment Video

Updated: Oct 12, 2025

2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes
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NAADP-binding proteins find their identity.

Jonathan S Marchant1, Gihan S Gunaratne1, Xinjiang Cai2

  • 1Department of Cell Biology, Neurobiology and Anatomy, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI 53226, USA.

Trends in Biochemical Sciences
|November 23, 2021
PubMed
Summary
This summary is machine-generated.

Nicotinic acid adenine dinucleotide phosphate (NAADP) activates calcium channels indirectly via NAADP-binding proteins. Two novel NAADP-binding proteins, JPT2 and LSM12, were recently identified, advancing understanding of this critical signaling pathway.

Keywords:
calcium signalingcancerendosomeslysosomesphotoaffinity probes

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Area of Science:

  • Cellular signaling
  • Ion channel regulation
  • Molecular biology

Background:

  • Nicotinic acid adenine dinucleotide phosphate (NAADP) is a crucial second messenger regulating intracellular calcium (Ca2+) release.
  • NAADP activates two-pore channels (TPCs) located on endosomes and lysosomes, but the direct binding site on TPCs remains elusive.
  • NAADP's mechanism involves indirect activation of TPCs through associated NAADP-binding proteins (NAADP-BPs).

Purpose of the Study:

  • To identify the NAADP-binding proteins (NAADP-BPs) responsible for mediating NAADP's action on TPCs.
  • To bridge the knowledge gap between NAADP signaling and TPC activation.
  • To provide new avenues for investigating and manipulating the NAADP signaling pathway.

Main Methods:

  • The abstract does not detail specific experimental methods but implies a search and identification process for NAADP-BPs.
  • The identification of Jupiter microtubule associated homolog 2 (JPT2) and like-Sm protein 12 (LSM12) as NAADP-BPs is highlighted.

Main Results:

  • Two novel NAADP-binding proteins, Jupiter microtubule associated homolog 2 (JPT2) and like-Sm protein 12 (LSM12), have been identified.
  • These proteins function as intermediaries in the NAADP signaling pathway, linking NAADP to TPC activation.
  • The identification of JPT2 and LSM12 resolves a long-standing question regarding NAADP's indirect mechanism.

Conclusions:

  • The discovery of JPT2 and LSM12 provides critical molecular players in NAADP-mediated calcium signaling.
  • These findings open new research directions for elucidating the precise molecular mechanisms of NAADP action on TPCs.
  • Understanding these NAADP-BPs will facilitate future therapeutic strategies targeting the NAADP pathway.