| First Author | Bendall AJ | Year | 1998 |
| Journal | Differentiation | Volume | 63 |
| Issue | 3 | Pages | 151-7 |
| PubMed ID | 9697309 | Mgi Jnum | J:49807 |
| Mgi Id | MGI:1278140 | Doi | 10.1046/j.1432-0436.1998.6330151.x |
| Citation | Bendall AJ, et al. (1998) Protein complex formation between Msx1 and Lhx2 homeoproteins is incompatible with DNA binding activity. Differentiation 63(3):151-7 |
| abstractText | Msx genes encode a family of homeoproteins that function as transcription repressors through protein-protein interactions. Here we show that Lhx2, a LIM-type homeoprotein, is a protein partner for Msx1 in vitro and in cellular extracts. The interaction between Msx1 and Lhx2 is mediated through the homeodomain-containing regions of both proteins. Interestingly, the LIM domains, which serve as protein interaction domains for other partners of Lhx2, are not required for the Msx1-Lhx2 association. We show that Msx1 and Lhx2 form a protein complex in the absence of DNA, and that DNA binding by either protein alone can occur at the expense of protein complex formation. The significance of this protein-protein interaction is underscored by the expression patterns of Msx1 and Lhx2, which are partially overlapping during murine embryogenesis. The description of Lhx2 as a protein partner for Msx1 suggests that the functional specificity of homeoproteins in vivo is determined by a balance between their association with DNA and their protein partners. |
