American Thyroid Association Guide to Investigating Thyroid Hormone Economy and Action in Rodent and Cell Models

Background: An in-depth understanding of the fundamental principles that regulate thyroid hormone homeostasis is critical for the development of new diagnostic and treatment ap-proaches for patients with thyroid disease. Summary: Important clinical practices in use today for the treatment of patients with hypothy-roidism, hyperthyroidism, or thyroid cancer, are the result of laboratory discoveries made by scientists investigating the most basic aspects of thyroid structure and molecular biology. In this document, a panel of experts commissioned by the American Thyroid Association makes a se-ries of recommendations related to the study of thyroid hormone economy and action. These recommendations are intended to promote standardization of study design, which should in turn increase the comparability and reproducibility of experimental findings. Conclusions: It is expected that adherence to these recommendations by investigators in the field will facilitate progress towards a better understanding of the thyroid gland and thyroid hormone dependent processes

Phosphorylation of tubulin enhances its interaction with membranes

Tubulin, the main component of intracellular microtubules, is also a major protein in subcellular membrane preparations1–4 and can interact with biological5–7 and artificial8–12 membranes in vitro. Of particular interest is the association of tubulin with postsynaptic junctional lattices enriched in a polypeptide of relative molecular mass (Mr) 50,000 (50K)13, recently identified as the major subunit of the calmodulin-dependent protein kinase14. Phosphorylation of tubulin with a calmodulin-dependent protein kinase similar to that found in postsynaptic densities inhibits its ability to self-assemble into microtubules in a reversible fashion15. This involves the phosphorylation of residues in its 4K carboxy-terminal region, a domain that seems to regulate its self-assembly16–18. The results presented here suggest that the phosphorylation of tubulin with this kinase enhances its ability to interact with membranes. This effect is reversible.Peer reviewe