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

Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Catenins01:23

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...

You might also read

Related Articles

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

Sort by
Same author

Human CD8-iTreg are potent GVHD suppressors and tumoricidal effectors by release of Granzyme-K <sup>+</sup> Supramolecular Attack Particles.

bioRxiv : the preprint server for biology·2026
Same author

Stoichiometrically Defined Antibody-DNA Conjugates for Quantitative Super-Resolution Imaging.

Nano letters·2026
Same author

PD-1 signaling and PD-1 blockade-mediated tumor control are established at microvillar T cell contacts.

Science immunology·2026
Same author

Kv1.3 palmitoylation regulates spatial distribution and channel removal from the immunological synapse.

Cellular and molecular life sciences : CMLS·2026
Same author

Psychosocial and behavioral correlates of persistent pain post disease-modifying treatment change in rheumatoid arthritis: a 12-month cohort study.

Advances in rheumatology (London, England)·2026
Same author

Mixed-mobility supported lipid bilayers uncover the role of immobilized ICAM1 on T cell activation and immune synapse organization.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

ZNRF3 and RNF43 are active monomeric E3 ubiquitin ligases that self-associate.

Science signaling·2026
Same journal

Allosteric ligands with distinct properties uncover tissue-specific physiological regulation mediated by free fatty acid receptor 2.

Science signaling·2026
Same journal

Diacylglycerol kinase ζ in B lymphocytes supports CD40-mediated immune synapse formation, mTORC1 signaling, and plasma cell fate.

Science signaling·2026
Same journal

The APC/C adaptor Cdh1 stabilizes STING to potentiate innate immune activation in renal cell carcinoma.

Science signaling·2026
Same journal

Fattening mother's milk with oxytocin.

Science signaling·2026
Same journal

Virion display reveals MD-1 as an endogenous agonist for the orphan receptor GPRC5B.

Science signaling·2026
See all related articles

Related Experiment Video

Updated: Jun 11, 2026

Qualitative and Quantitative Analysis of the Immune Synapse in the Human System Using Imaging Flow Cytometry
08:35

Qualitative and Quantitative Analysis of the Immune Synapse in the Human System Using Imaging Flow Cytometry

Published on: January 7, 2019

PTPN22 regulates T cell synapse formation through PSTPIP1-dependent actin remodeling.

Megan D Joseph1, Cecilia Zaza1, Olivia P L Dalby1,2

  • 1London Centre for Nanotechnology, University College London, WC1H 0AH London, UK.

Science Signaling
|June 9, 2026
PubMed
Summary
This summary is machine-generated.

Protein tyrosine phosphatase nonreceptor type 22 (PTPN22) regulates T cell activation by interacting with PSTPIP1 to control cytoskeletal dynamics. Its deficiency causes aberrant actin remodeling and enhanced signaling, offering insights into autoimmune diseases.

More Related Videos

Spatial and Temporal Control of T Cell Activation Using a Photoactivatable Agonist
07:48

Spatial and Temporal Control of T Cell Activation Using a Photoactivatable Agonist

Published on: April 25, 2018

Purification of the Dendritic Filopodia-rich Fraction
11:51

Purification of the Dendritic Filopodia-rich Fraction

Published on: May 2, 2019

Related Experiment Videos

Last Updated: Jun 11, 2026

Qualitative and Quantitative Analysis of the Immune Synapse in the Human System Using Imaging Flow Cytometry
08:35

Qualitative and Quantitative Analysis of the Immune Synapse in the Human System Using Imaging Flow Cytometry

Published on: January 7, 2019

Spatial and Temporal Control of T Cell Activation Using a Photoactivatable Agonist
07:48

Spatial and Temporal Control of T Cell Activation Using a Photoactivatable Agonist

Published on: April 25, 2018

Purification of the Dendritic Filopodia-rich Fraction
11:51

Purification of the Dendritic Filopodia-rich Fraction

Published on: May 2, 2019

Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • Protein tyrosine phosphatase nonreceptor type 22 (PTPN22) is a critical negative regulator of T cell activation and immune tolerance.
  • The autoimmune disease-associated R620W variant of PTPN22 suggests its role in T cell responses.
  • Understanding PTPN22's function is crucial for insights into immune dysregulation and autoimmune diseases.

Purpose of the Study:

  • To investigate the role of PTPN22 in modulating T cell activation and cytoskeletal dynamics.
  • To elucidate the interaction between PTPN22 and proline-serine-threonine phosphatase-interacting protein 1 (PSTPIP1) in T cell signaling.
  • To explore the impact of PTPN22 deficiency on actin remodeling and T cell receptor (TCR) signaling.

Main Methods:

  • Utilized Jurkat cell models to study T cell activation.
  • Investigated the interaction between PTPN22 and PSTPIP1 at the immunological synapse.
  • Employed super-resolution DNA-PAINT to analyze nanoscale protein organization and TCR clustering.
  • Assessed actin remodeling and calcium signaling in response to TCR stimulation.

Main Results:

  • PTPN22 modulates cytoskeletal dynamics at the immunological synapse via interaction with PSTPIP1.
  • PTPN22 deficiency disrupts Arp2/3-dependent actin remodeling, leading to excessive F-actin foci and PSTPIP1 mislocalization.
  • Loss of PTPN22 enhances calcium signaling, particularly under low-affinity TCR stimulation.
  • Super-resolution analysis revealed aberrant PSTPIP1-TCR colocalization and increased TCR clustering in PTPN22-deficient cells.

Conclusions:

  • A novel PTPN22-PSTPIP1 signaling axis is identified, critical for regulating cytoskeletal remodeling and receptor organization in T cells.
  • PTPN22 plays a key role in maintaining T cell homeostasis by controlling actin dynamics and TCR signaling.
  • Dysregulation of this PTPN22-PSTPIP1 pathway may contribute to T cell hyperactivation and autoimmune diseases.