| Title | Cell signaling and function organized by PB1 domain interactions. |
| Publication Type | Journal Article |
| Year of Publication | 2006 |
| Authors | Moscat J, Diaz-Meco MT, Albert A, Campuzano S |
| Journal | Mol Cell |
| Volume | 23 |
| Issue | 5 |
| Pagination | 631-40 |
| Date Published | 2006 Sep 01 |
| ISSN | 1097-2765 |
| Keywords | Adaptor Proteins, Signal Transducing, Animals, DNA-Binding Proteins, Humans, Inflammation, Nuclear Proteins, Protein Binding, Protein Structure, Tertiary, Proteins, Sequestosome-1 Protein, Signal Transduction, Transcription Factors |
| Abstract | The PB1-domain-containing proteins p62, aPKC, MEKK2/MEKK3, MEK5, and Par-6 play roles in critical cell processes like osteoclastogenesis, angiogenesis, and early cardiovascular development or cell polarity. PB1 domains are scaffold modules that adopt the topology of ubiquitin-like beta-grasp folds that interact with each other in a front-to-back mode to arrange heterodimers or homo-oligomers. The different PB1 domain adaptors provide specificity for PB1 kinases to ensure the effective transmission of cellular signals. Also, recent data suggest that PB1 domains may serve to orchestrate signaling cascades not involving other PB1 domains, such as the MEK5-ERK5 and p62-ERK1 interactions. |
| DOI | 10.1016/j.molcel.2006.08.002 |
| Alternate Journal | Mol Cell |
| PubMed ID | 16949360 |
Related Faculty:
Maria Diaz-Meco Conde, Ph.D.