Two Distinct Domains within CIITA Mediate Self-Association: Involvement of the GTP-Binding and Leucine-Rich Repeat Domains
AUTOR(ES)
Linhoff, Michael W.
FONTE
American Society for Microbiology
RESUMO
CIITA is the master regulator of class II major histocompatibility complex gene expression. We present evidence that CIITA can self-associate via two domains: the C terminus (amino acids 700 to 1130) and the GTP-binding domain (amino acids 336 to 702). Heterotypic and homotypic interactions are observed between these two regions. Deletions within the GTP-binding domain that reduce GTP-binding and transactivation function also reduce self-association. In addition, two leucine residues in the C-terminal leucine-rich repeat region are critical for self-association as well as function. This study reveals for the first time a complex pattern of CIITA self-association. These interactions are discussed with regard to the apoptosis signaling proteins, Apaf-1 and Nod1, which share domain arrangements similar to those of CIITA.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=86929Documentos Relacionados
- Binding site for Robo receptors revealed by dissection of the leucine-rich repeat region of Slit
- Multiple Functions of the Leucine-Rich Repeat Protein LrrA of Treponema denticola
- HAESA, an Arabidopsis leucine-rich repeat receptor kinase, controls floral organ abscission
- The relationship between the L1 and L2 domains of the insulin and epidermal growth factor receptors and leucine-rich repeat modules
- Self-Association of CIITA and Its Transactivation Potential