Abstract
The CD3ε proline-rich sequence (PRS) binds to the cytosolic adaptor molecule Nck after TCR ligation. It has been proposed that this interaction is essential for immunological synapse formation and T cell activation. To assess the physiological importance of the CD3ε PRS, we have generated mice that lack this motif (CD3ε.PRSM). Pull-down experiments demonstrated the inability of Nck to bind to the CD3ε PRS in thymocytes from mutant mice after TCR ligation. Surprisingly, no differences were observed in the number and percentage of T cell subsets in the thymus and spleen, and there was no apparent defect in positive or negative selection. Furthermore, the proliferative response of CD3ε.PRSM T cells to staphylococcal enterotoxin B and anti-CD3 Ab was normal. TCR surface expression, constitutive internalization, and Ag-induced down-modulation were also normal. These data suggest that the interaction between the CD3ε PRS and Nck, or any other Src homology 3 domain-containing molecule, is not essential for T cell development and function.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 270-275 |
| Number of pages | 6 |
| Journal | Journal of Immunology |
| Volume | 175 |
| Issue number | 1 |
| State | Published - Jul 1 2005 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Immunology
Cite this
The CD3ε proline-rich sequence, and its interaction with Nck, is not required for T cell development and function. / Szymczak, Andrea L.; Workman, Creg J.; Gil, Diana; Dilioglou, Smaroula; Vignali, Kate M.; Palmer, Ed; Vignali, D. A A.
In: Journal of Immunology, Vol. 175, No. 1, 01.07.2005, p. 270-275.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The CD3ε proline-rich sequence, and its interaction with Nck, is not required for T cell development and function
AU - Szymczak, Andrea L.
AU - Workman, Creg J.
AU - Gil, Diana
AU - Dilioglou, Smaroula
AU - Vignali, Kate M.
AU - Palmer, Ed
AU - Vignali, D. A A
PY - 2005/7/1
Y1 - 2005/7/1
N2 - The CD3ε proline-rich sequence (PRS) binds to the cytosolic adaptor molecule Nck after TCR ligation. It has been proposed that this interaction is essential for immunological synapse formation and T cell activation. To assess the physiological importance of the CD3ε PRS, we have generated mice that lack this motif (CD3ε.PRSM). Pull-down experiments demonstrated the inability of Nck to bind to the CD3ε PRS in thymocytes from mutant mice after TCR ligation. Surprisingly, no differences were observed in the number and percentage of T cell subsets in the thymus and spleen, and there was no apparent defect in positive or negative selection. Furthermore, the proliferative response of CD3ε.PRSM T cells to staphylococcal enterotoxin B and anti-CD3 Ab was normal. TCR surface expression, constitutive internalization, and Ag-induced down-modulation were also normal. These data suggest that the interaction between the CD3ε PRS and Nck, or any other Src homology 3 domain-containing molecule, is not essential for T cell development and function.
AB - The CD3ε proline-rich sequence (PRS) binds to the cytosolic adaptor molecule Nck after TCR ligation. It has been proposed that this interaction is essential for immunological synapse formation and T cell activation. To assess the physiological importance of the CD3ε PRS, we have generated mice that lack this motif (CD3ε.PRSM). Pull-down experiments demonstrated the inability of Nck to bind to the CD3ε PRS in thymocytes from mutant mice after TCR ligation. Surprisingly, no differences were observed in the number and percentage of T cell subsets in the thymus and spleen, and there was no apparent defect in positive or negative selection. Furthermore, the proliferative response of CD3ε.PRSM T cells to staphylococcal enterotoxin B and anti-CD3 Ab was normal. TCR surface expression, constitutive internalization, and Ag-induced down-modulation were also normal. These data suggest that the interaction between the CD3ε PRS and Nck, or any other Src homology 3 domain-containing molecule, is not essential for T cell development and function.
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UR - http://www.scopus.com/inward/citedby.url?scp=21244489949&partnerID=8YFLogxK
M3 - Article
C2 - 15972658
AN - SCOPUS:21244489949
VL - 175
SP - 270
EP - 275
JO - Journal of Immunology
JF - Journal of Immunology
SN - 0022-1767
IS - 1
ER -