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Related Concept Videos

Phosphorylation01:02

Phosphorylation

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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.
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The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
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Protein Kinases and Phosphatases02:54

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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.
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Updated: Jun 14, 2025

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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A phosphorylation-controlled switch confers cell cycle-dependent protein relocalization.

Xiaofu Cao1,2, Shiying Huang1,2, Mateusz M Wagner2,3

  • 1Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, USA.

Nature Cell Biology
|August 29, 2024
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Summary
This summary is machine-generated.

Researchers developed a novel mitosis-specific protein recruitment system using a PLEKHA5-derived module. This tool enables precise protein localization during cell division without external triggers, aiding the study of mitosis.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Protein localization studies are crucial for understanding cell function.
  • Existing tools for manipulating protein localization often rely on exogenous triggers, which can perturb sensitive cellular processes like mitosis.
  • Mitosis is a complex, highly regulated process sensitive to external stimuli.

Purpose of the Study:

  • To develop a novel system for mitosis-specific protein recruitment to the plasma membrane.
  • To overcome the limitations of exogenous triggers in studying mitosis.
  • To enable precise spatiotemporal manipulation of protein function during cell division.

Main Methods:

  • Exploited a phosphorylation-controlled, cell cycle-dependent localization of the adaptor protein PLEKHA5.
  • Engineered a 15 kDa module derived from PLEKHA5 for protein recruitment.
  • Utilized direct fusion or GFP-GFP nanobody interaction for cargo recruitment.
  • Developed a mitosis-enabled anchor-away/recruiter system.

Main Results:

  • Successfully developed a system for mitosis-specific protein recruitment to the plasma membrane.
  • The system requires no exogenous stimulus, avoiding interference with cell physiology.
  • Demonstrated applications including 'knock sideways' to remove proteins during mitosis and conditional recruitment of enzymes to alter lipid content.

Conclusions:

  • The mitosis-enabled anchor-away/recruiter system provides a powerful, non-perturbative tool for studying mitosis.
  • This system allows for precise temporal control of protein function during cell division.
  • Facilitates research into mitosis-specific protein functions and cellular processes without exogenous interference.