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Related Concept Videos

Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

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

Directing Proteins to the Rough Endoplasmic Reticulum

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...
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...
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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...
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...
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

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Related Experiment Video

Updated: Jun 25, 2026

Multi-color Localization Microscopy of Single Membrane Proteins in Organelles of Live Mammalian Cells
11:06

Multi-color Localization Microscopy of Single Membrane Proteins in Organelles of Live Mammalian Cells

Published on: June 30, 2018

Semi-supervised protein subcellular localization.

Qian Xu1, Derek Hao Hu, Hong Xue

  • 1Program of Bioengineering, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong. fleurxq@ust.hk

BMC Bioinformatics
|February 12, 2009
PubMed
Summary
This summary is machine-generated.

This study introduces semi-supervised learning for protein subcellular localization prediction, significantly reducing the need for labeled data. The novel approach enhances prediction accuracy compared to traditional methods.

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Area of Science:

  • Bioinformatics
  • Computational Biology
  • Molecular Biology

Background:

  • Protein subcellular localization is crucial for understanding protein function and cellular processes.
  • Accurate prediction aids genome annotation and drug target identification.
  • Current machine learning methods, like Support Vector Machines (SVMs), require extensive labeled data, which is costly and time-consuming to obtain.

Purpose of the Study:

  • To develop a computational method for predicting protein subcellular localization that minimizes the requirement for labeled data.
  • To leverage unlabeled data to improve the accuracy and efficiency of prediction models.

Main Methods:

  • Implementation of a semi-supervised learning framework.
  • Initial classifier construction using a small set of labeled protein examples.
  • Refinement of the classifier using a larger pool of unlabeled protein instances.

Main Results:

  • The semi-supervised approach effectively reduces the data labeling workload.
  • The proposed method significantly enhances the prediction performance of existing SVM classifiers.
  • Experimental results demonstrate a performance improvement exceeding 10% over state-of-the-art SVMs.

Conclusions:

  • Semi-supervised learning offers a viable solution for accurate protein subcellular localization prediction with reduced labeling effort.
  • This approach improves the efficiency and effectiveness of computational methods in bioinformatics.
  • The findings have implications for accelerating protein function prediction and genomic studies.