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The role of the Cdk9/Cyclin T1 complex in T cell differentiation
Author(s) -
Leucci Eleonora,
De Falco Giulia,
Onnis Anna,
Cerino Giovanna,
Cocco Mario,
Luzzi Anna,
Crupi Domenica,
Tigli Chiara,
Bellan Cristiana,
Tosi Piero,
Leoncini Lorenzo,
Giordano Antonio
Publication year - 2007
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.21032
Subject(s) - microbiology and biotechnology , cyclin , biology , cyclin a , cyclin a2 , cellular differentiation , cyclin d , cell , cyclin dependent kinase 2 , cell cycle , kinase , protein kinase a , gene , genetics
The Cdk9/Cyclin T1 complex is very important in controlling specific differentiative pathways of several cell types, including muscle cells and neurons. We recently demonstrated the involvement of this complex in B cell activation/differentiation. To check whether the Cdk9/Cyclin T1 complex is also involved in the T cell activation/differentiation process, we isolated different T cell populations by magnetic separation, based on their surface antigens. We observed that the expression level of Cdk9/Cyclin T1 increases in effector T cells (CD27 + ), as well as in activated T cells (CD25 + ) and memory T cells (CD45RA − ), thus suggesting a specific upregulation of the Cdk9/Cyclin T1 complex following antigen encounter. We have previously demonstrated that in B cells, Cdk9 interacts in vivo with the E2A gene products E12/E47 (members of the basic helix‐loop‐helix family) which are involved in differentiation. In this article, we show that this interaction also occurs in T cells. This suggests an active role for the Cdk9/Cyclin T1 complex during lymphoid differentiation, through physical binding with E12 and E47. These preliminary results suggest that the Cdk9/Cyclin T1 complex may be important in the activation and differentiation program of lymphoid cells and that its upregulation, which is due to still unknown mechanisms, may contribute to malignant transformation. J. Cell. Physiol. 212: 411–415, 2007. © 2007 Wiley‐Liss, Inc.