Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Eukaryotic Compartmentalization01:37

Eukaryotic Compartmentalization

11.0K
One of the distinguishing features of eukaryotic cells is that they contain membrane-bound organelles, such as the nucleus and mitochondria, that carry out specialized functions. Since biological membranes are only selectively permeable to solutes, they help create a compartment with controlled conditions inside an organelle. These microenvironments are tailored to the organelle's specific functions and help isolate them from the surrounding cytosol.
For example, lysosomes in the animal...
11.0K
Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

11.3K
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...
11.3K
Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

8.5K
Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
8.5K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

2.4K
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...
2.4K
Regulated mRNA Transport02:22

Regulated mRNA Transport

6.3K
In eukaryotes, transcription and translation are compartmentalized; an mRNA is first synthesized in the nucleus and then selectively transported to the cytoplasm for protein synthesis. Before transport, a pre-mRNA undergoes several steps of post-transcriptional modifications including splicing, 5' capping, and the addition of a poly-adenine tail. Various proteins bind to the pre-mRNA during these modifications. The mRNA transport takes place with the help of multiple proteins playing...
6.3K
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

4.6K
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...
4.6K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Why machine learning fails at mass spectrometry for small molecules.

Nature metabolism·2026
Same author

Reply to: Limited evidence of AI superiority in seasonal influenza vaccine strain selection.

Nature medicine·2026
Same author

Active RNA synthesis patterns nuclear condensates.

Cell systems·2026
Same author

Family Physicians' Views of Who They Are Accountable To and Current Quality Metrics.

JAMA network open·2026
Same author

Protein FID: improved evaluation of protein structure generative models.

Bioinformatics (Oxford, England)·2026
Same author

Bridging the gap: aligning clinical decision support regulation with clinical practice in the era of artificial intelligence.

The Lancet. Digital health·2026
Same journal

Layered social competition coordinates reproductive hierarchy formation in ants.

bioRxiv : the preprint server for biology·2026
Same journal

Combination epigenetic-targeted therapy increases the immunogenicity of poorly immunogenic sarcomas.

bioRxiv : the preprint server for biology·2026
Same journal

Loss of LanC-like proteins delays post-injury regeneration of aging skeletal muscles.

bioRxiv : the preprint server for biology·2026
Same journal

Integrative Transfer Network: Deep Transfer Learning Across Populations and Prediction Targets.

bioRxiv : the preprint server for biology·2026
Same journal

Confidence-supported label-free metabolic imaging with FPhaS phase autofluorescence microscopy.

bioRxiv : the preprint server for biology·2026
Same journal

Sequence-encoded autoinhibition couples mRNA decapping activity to phase separation.

bioRxiv : the preprint server for biology·2026
See all related articles

Related Experiment Video

Updated: Jun 28, 2025

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
14:02

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells

Published on: April 9, 2018

8.5K

Protein codes promote selective subcellular compartmentalization.

Henry R Kilgore1, Itamar Chinn2, Peter G Mikhael2

  • 1Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.

Biorxiv : the Preprint Server for Biology
|April 25, 2024
PubMed
Summary
This summary is machine-generated.

Scientists discovered a hidden code within protein sequences that directs proteins to specific cellular compartments. This protein localization code ensures proteins with shared functions assemble correctly, impacting cell function and disease.

More Related Videos

Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System
11:47

Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System

Published on: August 1, 2016

16.0K
Subcellular Fractionation for ERK Activation Upon Mitochondrial-derived Peptide Treatment
07:55

Subcellular Fractionation for ERK Activation Upon Mitochondrial-derived Peptide Treatment

Published on: September 25, 2017

7.8K

Related Experiment Videos

Last Updated: Jun 28, 2025

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
14:02

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells

Published on: April 9, 2018

8.5K
Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System
11:47

Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System

Published on: August 1, 2016

16.0K
Subcellular Fractionation for ERK Activation Upon Mitochondrial-derived Peptide Treatment
07:55

Subcellular Fractionation for ERK Activation Upon Mitochondrial-derived Peptide Treatment

Published on: September 25, 2017

7.8K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Bioinformatics

Background:

  • Cells must precisely localize billions of proteins to specific compartments for proper function.
  • Proteins with shared functions need to efficiently assemble in designated subcellular locations.

Purpose of the Study:

  • To investigate if amino acid sequences contain codes for subcellular protein localization.
  • To develop a predictive model for protein compartment destination.
  • To explore the role of this code in protein assembly and disease.

Main Methods:

  • Development of a protein language model, ProtGPS, trained on human protein sequences.
  • Prediction of subcellular localization for proteins not included in the training set.
  • Generation of novel protein sequences guided by ProtGPS for targeted compartment assembly.
  • Identification of mutations affecting protein localization codes.

Main Results:

  • Proteins with shared functions utilize common amino acid sequence codes for compartment targeting.
  • The ProtGPS model accurately predicts subcellular localization of human proteins.
  • ProtGPS successfully guided the creation of novel proteins that assemble in specific compartments.
  • Pathological mutations altering this code were identified, leading to mislocalized proteins.

Conclusions:

  • Protein sequences encode a previously unrecognized 'distribution code' for subcellular localization, in addition to the 'folding code'.
  • This code is crucial for the assembly of functional protein complexes within cells.
  • Alterations in this protein localization code can contribute to disease pathogenesis.