| First Author | Xing Y | Year | 2004 |
| Journal | J Biol Chem | Volume | 279 |
| Issue | 29 | Pages | 30662-9 |
| PubMed ID | 15126499 | Mgi Jnum | J:91618 |
| Mgi Id | MGI:3047534 | Doi | 10.1074/jbc.M404107200 |
| Citation | Xing Y, et al. (2004) Structural basis of membrane targeting by the Phox homology domain of cytokine-independent survival kinase (CISK-PX). J Biol Chem 279(29):30662-9 |
| abstractText | The cytokine-independent survival kinase (CISK) in the serum and glucocorticoid-regulated kinase family plays an important role in mediating cell growth and survival. N-terminal to its catalytic kinase domain, CISK contains a phox homology (PX) domain, a phosphoinositide-binding motif that directs the membrane localization of CISK and regulates CISK activity. We have determined the crystal structures of the mouse CISK-PX domain to unravel the structural basis of membrane targeting of CISK. In addition to the specific interactions conferred by the phosphoinositide-binding pocket, the structure suggests that a hydrophobic loop region and a hydrophilic beta-turn contribute to the interactions with the membrane. Furthermore, biochemical studies reveal that CISK-PX dimerizes in the presence of the linker between the PX domain and kinase domain, suggesting a multivalent mechanism in membrane localization of CISK. |
