| First Author | Lin JH | Year | 1999 |
| Journal | J Biol Chem | Volume | 274 |
| Issue | 21 | Pages | 14706-15 |
| PubMed ID | 10329666 | Mgi Jnum | J:55090 |
| Mgi Id | MGI:1337221 | Doi | 10.1074/jbc.274.21.14706 |
| Citation | Lin JH, et al. (1999) The ankyrin repeat-containing adaptor protein Tvl-1 is a novel substrate and regulator of Raf-1. J Biol Chem 274(21):14706-15 |
| abstractText | Tvl-1 is a 269-amino acid ankyrin repeat protein expressed primarily in thymus, lung, and testes that was identified by screening a murine T-cell two-hybrid cDNA library for proteins that associate with the serine-threonine kinase Raf-1. The interaction of Tvl-1 with Raf-1 was confirmed by co-immunoprecipitation of the two proteins from COS-1 cells transiently transfected with Tvl-1 and Raf-1 expression constructs as well as by co-immunoprecipitation of the endogenous proteins from CV-1 and NB2 cells. Tvl-1 interacts with Raf-1 via its carboxyl-terminal ankyrin repeat domain. The same domain also mediates Tvl-1 homodimerization. Tvl-1 was detected by immunofluorescence in both the cytoplasm and the nucleus suggesting that in addition to Raf-1 it may also interact with nuclear proteins. Activated Raf-1 phosphorylates Tvl-1 both in vitro and in vivo. In baculovirus-infected Sf9 insect cells, Tvl-1 potentiates the activation of Raf-1 by Src and Ras while in COS-1 cells it potentiates the activation of Raf-1 by EGF. These data suggest that Tvl-1 is both a target as well as a regulator of Raf-1. The human homologue of Tvl-1 maps to chromosome 19p12, upstream of MEF2B with the two genes in a head to head arrangement. |
