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Related Concept Videos

Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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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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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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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...
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Updated: Jan 14, 2026

Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
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Modulating Subcellular Localization to Preserve the Stability and Functionality of Intracellular Nanobodies.

Wenli Sun1, Keke Huang1, Yaping Cheng1

  • 1Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), Shanghai Institute of Infectious Disease and Biosecurity, School of Basic Medical Sciences, Fudan University, Shanghai 200032, China.

Antibodies (Basel, Switzerland)
|October 24, 2025
PubMed
Summary
This summary is machine-generated.

Engineered nanobodies fused with localization motifs show enhanced stability and reduced degradation within cells. This strategy improves nanobody efficacy for intracellular applications in research and therapeutics.

Keywords:
intracellular deliverylocalization motifnanobodyprotein stabilitysubcellular localization

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Area of Science:

  • Biotechnology
  • Molecular Biology
  • Cell Biology

Background:

  • Antibodies are crucial for therapeutics and diagnostics but limited to extracellular targets.
  • Intracellular delivery and stability pose challenges for antibody applications.
  • Nanobodies offer potential for intracellular use but suffer from aggregation and degradation.

Purpose of the Study:

  • To engineer nanobodies for enhanced intracellular stability and efficacy.
  • To overcome limitations of nanobody degradation and aggregation in the cytosol.
  • To expand nanobody applications in intracellular research and therapy.

Main Methods:

  • Engineered nanobodies by fusing them with subcellular localization motifs.
  • Redirected nanobody localization to specific cellular compartments like the cytoskeleton and endomembrane system.
  • Assessed nanobody stability, degradation rates, target-binding capacity, and ubiquitination levels.

Main Results:

  • Cytoskeletal and endomembrane-localized nanobodies showed significantly reduced degradation.
  • Engineered nanobodies exhibited enhanced stability while retaining target-binding capacity.
  • Modifications led to lower ubiquitination levels and prolonged functional activity.

Conclusions:

  • A novel strategy was developed to enhance intracellular nanobody stability and efficacy.
  • This approach broadens the potential of nanobodies in functional proteomics and disease research.
  • The findings support the development of nanobody-based therapeutics for intracellular targets.