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Related Concept Videos

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...
Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

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...
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...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...

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Related Experiment Video

Updated: Jun 5, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Phosphorylation meets nuclear import: a review.

Jonathan D Nardozzi1, Kaylen Lott, Gino Cingolani

  • 1Dept, of Biochemistry and Molecular Biology, Thomas Jefferson University, 233 South 10th Street, Philadelphia, PA 19107, USA. gino.cingolani@jefferson.edu.

Cell Communication and Signaling : CCS
|December 25, 2010
PubMed
Summary

Phosphorylation, a key biological process, regulates how molecules move between the nucleus and cytoplasm. This review clarifies how this modification impacts nucleocytoplasmic trafficking and cellular functions.

More Related Videos

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Related Experiment Videos

Last Updated: Jun 5, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Phosphorylation is a widespread regulatory modification crucial for numerous biological pathways.
  • Nucleocytoplasmic transport is vital for cellular function and implicated in disease.
  • Phosphorylation of cargo molecules influences their nuclear availability, impacting gene expression and cell growth.

Purpose of the Study:

  • To review and clarify the role of phosphorylation in nucleocytoplasmic trafficking.
  • To provide general rules for understanding how reversible phosphorylation affects substrate localization.
  • To address the confusing and often contradictory findings in the current literature.

Main Methods:

  • Literature review of key findings in the field of phosphorylation and nucleocytoplasmic transport.
  • Analysis of existing studies on the effects of phosphorylation and dephosphorylation on cargo transport.
  • Synthesis of information to establish general regulatory principles.

Main Results:

  • Phosphorylation's effect on nucleocytoplasmic trafficking can be complex and context-dependent.
  • Opposite effects of phosphorylation and dephosphorylation on cargo transport have been observed.
  • A clear understanding of how phosphate group attachment influences biological response is emerging.

Conclusions:

  • Reversible phosphorylation is a critical regulatory mechanism for nucleocytoplasmic localization.
  • Understanding these phosphorylation-dependent mechanisms is essential for comprehending gene expression, cell growth, and disease.
  • This review aims to consolidate current knowledge and provide a framework for future research in this area.