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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...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
Signal Sequences and Sorting Receptors01:41

Signal Sequences and Sorting Receptors

Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
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...
Bacterial Translocation and Protein Secretion01:26

Bacterial Translocation and Protein Secretion

Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...

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Related Experiment Video

Updated: Jun 8, 2026

Cell-Type Specific Protein Purification and Identification from Complex Tissues Using a Mutant Methionine tRNA Synthetase Mouse Line
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Published on: April 13, 2022

Trans-SILAC: sorting out the non-cell-autonomous proteome.

Oded Rechavi1, Matan Kalman, Yuan Fang

  • 1Department of Neurobiology, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.

Nature Methods
|October 12, 2010
PubMed
Summary
This summary is machine-generated.

Researchers developed a new proteomics method called trans-SILAC to identify proteins transferred between cells or from pathogens. This technique helps understand cellular communication and infection dynamics by quantifying protein exchange.

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Area of Science:

  • Proteomics
  • Cell Biology
  • Microbiology

Background:

  • Identifying non-cell-autonomous proteins transferred between cells or from pathogens is challenging.
  • Understanding protein exchange is crucial for cell-cell communication and host-pathogen interactions.

Purpose of the Study:

  • To develop a quantitative proteomics approach for identifying non-cell-autonomous proteins.
  • To establish a method for analyzing protein transfer between cells and from pathogens.

Main Methods:

  • Utilized stable-isotope labeling of amino acids in cell culture (SILAC).
  • Combined SILAC with high-purity cell sorting and bioinformatics analysis.
  • Developed the 'trans-SILAC' methodology.

Main Results:

  • Discovered numerous proteins transferred from human B cells to natural killer cells.
  • Quantified the biosynthesis rates of Salmonella enterica proteins within infected human cells.
  • Successfully identified a repertoire of non-cell-autonomous proteins.

Conclusions:

  • Trans-SILAC is an effective method for examining protein exchange between cells.
  • The method is valuable for studying protein transfer in multicellular organisms and host-pathogen systems.
  • Provides insights into cellular communication and pathogen dynamics.