Functional Cooperation between the Proteins Nck and ADAP Is Fundamental for Actin Reorganization
In: Molecular and Cellular Biology, Jg. 31 (2011-07-01), S. 2653-2666
Online
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Zugriff:
T cell antigen receptor (TCR) activation triggers profound changes in the actin cytoskeleton. In addition to controlling cellular shape and polarity, this process regulates vital T cell responses, such as T cell adhesion, motility, and proliferation. These depend on the recruitment of the signaling proteins Nck and Wiskott-Aldrich syndrome protein (WASp) to the site of TCR activation and on the functional properties of the adapter proteins linker for activation of T cells (LAT) and SH2-domain-containing leukocyte protein of 76 kDa (SLP76). We now demonstrate that Nck is necessary but insufficient for the recruitment of WASp. We show that two pathways lead to SLP76-dependent actin rearrangement. One requires the SLP76 acidic domain, crucial to association with the Nck SH2 domain, and another requires the SLP76 SH2 domain, essential for interaction with the adhesion- and degranulation-promoting adapter protein ADAP. Functional cooperation between Nck and ADAP mediates SLP76-WASp interactions and actin rearrangement. We also reveal the molecular mechanism linking ADAP to actin reorganization.
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Functional Cooperation between the Proteins Nck and ADAP Is Fundamental for Actin Reorganization
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Autor/in / Beteiligte Person: | Fried, Sophie ; Barda-Saad, Mira ; Reicher, Barak ; Perl, Orly ; Pauker, Maor H. |
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Zeitschrift: | Molecular and Cellular Biology, Jg. 31 (2011-07-01), S. 2653-2666 |
Veröffentlichung: | Informa UK Limited, 2011 |
Medientyp: | unknown |
ISSN: | 1098-5549 (print) |
DOI: | 10.1128/mcb.01358-10 |
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