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 Experiment Videos

Ezrin is a substrate for Lck in T cells.

Matti Autero1, Leena Heiska, Lars Rönnstrand

  • 1Department of Biosciences, Division of Biochemistry, University of Helsinki, Helsinki, Finland.

FEBS Letters
|February 1, 2003
PubMed
Summary

The Lck tyrosine kinase regulates ezrin phosphorylation, a key protein in T cell activation. This study identifies ezrin as the first cytoskeletal substrate for Lck, revealing a novel mechanism in immune cell signaling.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Csk binding to integrin β3 is regulated by tyrosine and threonine phosphorylation of β3.

FEBS letters·2026
Same author

Association of iron metabolism with disease severity in acute Puumala hantavirus infection.

BMC nephrology·2025
Same author

Understanding the characteristic behaviour of the wild-type and mutant structure of FLT3 protein by computational methods.

Computational and structural biotechnology journal·2025
Same author

XeroGraph: enhancing data integrity in the presence of missing values with statistical and predictive analysis.

Bioinformatics advances·2025
Same author

Hypoxia favors tumor growth in colorectal cancer in an integrin αDβ1/hemoglobin δ-dependent manner.

Life science alliance·2024
Same author

Circulating mucosal-like IgA responses increase with severity of Puumala orthohantavirus-caused hemorrhagic fever with renal syndrome.

Frontiers in immunology·2024

Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • T cell activation involves early signaling events mediated by Lck tyrosine kinase.
  • Ezrin is a membrane-cytoskeleton linker protein crucial for cell structure and function.

Purpose of the Study:

  • To investigate the role of Lck tyrosine kinase in the regulation of ezrin phosphorylation.
  • To identify ezrin as a potential substrate for Lck.

Main Methods:

  • Utilized wild-type, CD45-deficient, and Lck-deficient Jurkat T cells.
  • Performed in vitro kinase assays with Lck and ezrin.
  • Employed tyrosine kinase and phosphatase inhibitors (PP2, pervanadate).

Main Results:

  • Ezrin was constitutively tyrosine phosphorylated in wild-type and CD45-deficient cells, but not in Lck-deficient cells.

Related Experiment Videos

  • Lck activity restoration led to ezrin phosphorylation.
  • Lck directly phosphorylated ezrin in vitro, with Y145 identified as the major phosphotyrosine site.

    • Conclusions:

    • Ezrin is identified as the first cytoskeletal substrate for Lck tyrosine kinase.
    • This finding elucidates a novel regulatory pathway in T cell activation involving Lck and ezrin.