ArticleCommunicative & integrative biology2011
Studies of novel interactions between Nck and VAV SH3 domains.
Article in Communicative & integrative biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- The Role of the Cytoskeleton in Regulating the Natural Killer Cell Immune Response in Health and Disease: From Signaling Dynamics to Function.Frontiers in cell and developmental biology · 2021Review
- Binding of Staphylococcal Enterotoxin B (SEB) to B7 Receptors Triggers TCR- and CD28-Mediated Inflammatory Signals in the Absence of MHC Class II Molecules.Frontiers in immunology · 2021Article
- A non-conserved amino acid variant regulates differential signalling between human and mouse CD28.Nature communications · 2018Article
- Actin retrograde flow controls natural killer cell response by regulating the conformation state of SHP-1.The EMBO journal · 2018Article
- Ubiquitylation-dependent negative regulation of WASp is essential for actin cytoskeleton dynamics.Molecular and cellular biology · 2012Article
- Stoichiometry of Nck-dependent actin polymerization in living cells.The Journal of cell biology · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Following T-cell antigen receptor (TCR) engagement, a multi-molecular complex consisting of SLP-76, Nck and VAV1 is formed and recruited to the T-cell antigen-presenting-cell (APC) interaction site. This complex is crucial for the regulation of the actin machinery. The molecules Nck (an adaptor) and VAV1 (a GEF for small G-proteins) were previously shown to bind SLP-76. Using high-resolution imaging techniques, together with gene silencing and biochemical analysis, we studied the dynamics of this signaling complex formation. We recently showed that VAV1 and Nck can bind each other independently of SLP-76. This direct interaction is mediated by the binding of the Nck C-terminal SH3 domain and the VAV1 N-terminal SH3 domain. This interaction contributes to the cooperative nature of the complex formation. This observation was confirmed in functional studies: disruption of the Nck-VAV1 interaction strongly inhibited actin polymerization. Here, we show that Nck-VAV1 interaction is not required for Ca(2+) mobilization, since a point mutation in the VAV1 N-terminal SH3 domain, which prevents the direct interaction between Nck and VAV1, has no effect on Ca(2+) flux and minimal effects on ZAP-70, LAT or PLCγ1 phosphorylation.
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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.