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Related Concept Videos

Subcellular Fractionation01:32

Subcellular Fractionation

8.1K
The homogenate obtained after cell lysis contains various membrane-bound organelles that can be further separated into pure fractions by subcellular fractionation. These isolates are used to study specific cellular components, analyze localized protein activity, and are even employed in diagnostics. Fractionation is typically achieved using centrifugation methods, the most common being density-gradient and differential centrifugation.
Differential Centrifugation
Differential centrifugation is...
8.1K
Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

18.5K
Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
Protein sorting can be of two types: signal-based sorting and vesicle-based trafficking. In signal-based sorting, specific amino acid sequences called sorting signals target proteins to the proper location inside the cell either via gated transport or by protein translocation.  In gated transport, folded...
18.5K
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

5.5K
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...
5.5K
Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

6.8K
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...
6.8K
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

13.9K
The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
13.9K
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

6.6K
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
6.6K

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Related Experiment Video

Updated: Oct 29, 2025

Enriching Subcellular Proteins in Leptospira Using a Triton X-114-Based Fractionation Approach
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Protein Subcellular Localization Prediction.

Elettra Barberis1,2, Emilio Marengo3,2, Marcello Manfredi4,5

  • 1Department of Translational Medicine, University of Piemonte Orientale, Novara, Italy.

Methods in Molecular Biology (Clifton, N.J.)
|July 8, 2021
PubMed
Summary
This summary is machine-generated.

Understanding protein subcellular localization is crucial for function. Recent advances in proteomics and bioinformatics offer accurate, efficient methods for determining protein location, interactions, and functions.

Keywords:
Protein subcellular localization predictionSample preparation protocolsSoftware for predictionSpatial proteomics

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Area of Science:

  • Proteomics
  • Cell Biology
  • Bioinformatics

Background:

  • Protein function is intrinsically linked to its subcellular localization and cellular microenvironment.
  • Accurate determination of protein localization is essential for understanding cellular processes.
  • Traditional methods for protein localization can be time-consuming and costly.

Purpose of the Study:

  • To introduce the importance of protein subcellular localization.
  • To discuss various proteomics techniques and computational methods for identifying protein localization.
  • To present recent advancements in spatial proteomics.

Main Methods:

  • Review of sample preparation protocols for proteomics.
  • Discussion of established and emerging proteomic techniques.
  • Analysis of data analysis strategies and software for protein localization prediction.
  • Overview of advanced spatial proteomics techniques.

Main Results:

  • Proteomics and bioinformatics have yielded effective techniques for protein localization.
  • Technological progress has led to more accurate and simpler workflows.
  • Spatial proteomics offers advanced capabilities for determining protein location.

Conclusions:

  • Knowledge of protein subcellular localization is fundamental for biological research.
  • A combination of experimental and computational approaches enhances localization accuracy.
  • Emerging spatial proteomics techniques provide deeper insights into protein function within cells.