| Autor: |
Cartwright, Natalia G., Kashyap, Anuj K., Schaefer, Brian C. |
| Zdroj: |
Molecular Biology of the Cell; September 2011, Vol. 22 Issue: 18 p3491-3497, 7p |
| Abstrakt: |
Protein kinase C{theta} (PKC{theta}) is a serine/threonine kinase that plays an essential role in antigen-regulated responses of T lymphocytes. Upon antigen stimulation, PKC{theta} is rapidly recruited to the immunological synapse (IS), the region of contact between the T cell and antigen-presenting cell. This behavior is unique among T cell PKC isoforms. To define domains of PKC{theta} required for retention at the IS, we generated deletion and point mutants of PKC{theta}. We used quantitative imaging analysis to assess IS retention of PKC{theta} mutants in antigen-stimulated T cell clones. Deletion of the kinase domain or site-directed mutation of a subset of known PKC{theta} phosphorylation sites abrogated or significantly reduced IS retention, respectively. IS retention did not correlate with phosphorylation of specific PKC{theta} residues but rather with kinase function. Thus PKC{theta} catalytic competence is essential for stable IS retention. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
