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Related Concept Videos

Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

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.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
Nuclear Export01:42

Nuclear Export

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...
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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...
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...

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Detecting Protein Subcellular Localization by Green Fluorescence Protein Tagging and 4',6-Diamidino-2-phenylindole Staining in Caenorhabditis elegans
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A functional nuclear localization sequence in the C. elegans TRPV channel OCR-2.

Meredith J Ezak1, Denise M Ferkey

  • 1Department of Biological Sciences, State University of New York at Buffalo, Buffalo, New York, United States of America.

Plos One
|September 30, 2011
PubMed
Summary
This summary is machine-generated.

Scientists found a nuclear localization sequence in the OCR-2 transient receptor potential vanilloid (TRPV) channel. This suggests TRPV channels may directly regulate neuronal gene expression within the nucleus.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • Gene expression modulation is vital for nervous system development and function.
  • Calcium signaling pathways translate cellular stimuli into transcriptional changes.
  • Mammalian Ca(v)1.2 calcium channels can enter the nucleus and act as transcription factors.

Purpose of the Study:

  • To identify mechanisms by which TRPV channels regulate neuronal gene expression.
  • To investigate a potential direct nuclear role for the C. elegans OCR-2 TRPV channel.

Main Methods:

  • Identification of a nuclear localization sequence (NLS) in the OCR-2 channel.
  • Functional assays to test NLS activity using a reporter protein.
  • Subcellular localization studies of OCR-2 channel fragments and full-length channel.

Main Results:

  • A functional NLS was identified in the C. elegans OCR-2 TRPV channel.
  • The NLS directed nuclear accumulation of a reporter protein and the OCR-2 C-terminus.
  • A portion of the full-length OCR-2 channel was found to localize to the nucleus in neuronal cells.

Conclusions:

  • The OCR-2 TRPV channel possesses a functional NLS, enabling nuclear import.
  • These findings suggest a direct nuclear function for OCR-2 in regulating neuronal gene expression.
  • This expands the known roles of calcium channels in transcriptional regulation.