ArticleMolecular and cellular biology2014
Binding of WIP to actin is essential for T cell actin cytoskeleton integrity and tissue homing.
Article in Molecular and cellular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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The trial behind it
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- The role of actin cytoskeleton CFL1 and ADF/cofilin superfamily in inflammatory response.Frontiers in molecular biosciences · 2024Review
- CD28 and chemokine receptors: Signalling amplifiers at the immunological synapse.Frontiers in immunology · 2022Review
- Imaging Cytoskeleton Components by Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Actin Dynamics at the T Cell Synapse as Revealed by Immune-Related Actinopathies.Frontiers in cell and developmental biology · 2021Review
- The Disordered Cellular Multi-Tasker WIP and Its Protein-Protein Interactions: A Structural View.Biomolecules · 2020Review
- The Lack of WIP Binding to Actin Results in Impaired B Cell Migration and Altered Humoral Immune Responses.Cell reports · 2018Article
- Cytoskeletal control of B cell responses to antigens.Nature reviews. Immunology · 2017Review
- A DOCK8-WIP-WASp complex links T cell receptors to the actin cytoskeleton.The Journal of clinical investigation · 2016Article
- Article
- Human Immunodeficiencies Related to Defective APC/T Cell Interaction.Frontiers in immunology · 2015Review
- T Lymphocyte Migration: An Action Movie Starring the Actin and Associated Actors.Frontiers in immunology · 2015Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
The Wiskott-Aldrich syndrome protein (WASp) is important for actin polymerization in T cells and for their migration. WASp-interacting protein (WIP) binds to and stabilizes WASp and also interacts with actin. Cytoskeletal and functional defects are more severe in WIP(-/-) T cells, which lack WASp, than in WASp(-/-) T cells, suggesting that WIP interaction with actin may be important for T cell cytoskeletal integrity and function. We constructed mice that lack the actin-binding domain of WIP (WIPΔABD mice). WIPΔABD associated normally with WASp but not F-actin. T cells from WIPΔABD mice had normal WASp levels but decreased cellular F-actin content, a disorganized actin cytoskeleton, impaired chemotaxis, and defective homing to lymph nodes. WIPΔABD mice exhibited a T cell intrinsic defect in contact hypersensitivity and impaired responses to cutaneous challenge with protein antigen. Adoptively transferred antigen-specific CD4(+) T cells from WIPΔABD mice had decreased homing to antigen-challenged skin of wild-type recipients. These findings show that WIP binding to actin, independently of its binding to WASp, is critical for the integrity of the actin cytoskeleton in T cells and for their migration into tissues. Disruption of WIP binding to actin could be of therapeutic value in T cell-driven inflammatory diseases.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.