| First Author | Behrends J | Year | 2005 |
| Journal | Mol Cell Biol | Volume | 25 |
| Issue | 7 | Pages | 2846-52 |
| PubMed ID | 15767687 | Mgi Jnum | J:97638 |
| Mgi Id | MGI:3575968 | Doi | 10.1128/MCB.25.7.2846-2852.2005 |
| Citation | Behrends J, et al. (2005) Normal thyroid structure and function in rhophilin 2-deficient mice. Mol Cell Biol 25(7):2846-52 |
| abstractText | Rhophilin 2 is a Rho GTPase binding protein initially isolated by differential screening of a chronically thyrotropin (TSH)-stimulated dog thyroid cDNA library. In thyroid cell culture, expression of rhophilin 2 mRNA and protein is enhanced following TSH stimulation of the cyclic AMP (cAMP) transduction cascade. Yeast two-hybrid screening and coimmunoprecipitation have revealed that the GTP-bound form of RhoB and components of the cytoskeleton are protein partners of rhophilin 2. These results led us to suggest that rhophilin 2 could play an important role downstream of RhoB in the control of endocytosis during the thyroid secretory process which follows stimulation of the TSH/cAMP pathway. To validate this hypothesis, we generated rhophilin 2-deficient mice and analyzed their thyroid structure and function. Mice lacking rhophilin 2 develop normally, have normal life spans, and are fertile. They have no visible goiter and no obvious clinical signs of hyper- or hypothyroidism. The morphology of thyroid cells and follicles in these mice were normal, as were the different biological tests performed to investigate thyroid function. Our results indicate that rhophilin 2 does not play an essential role in thyroid physiology. |
