Disease relevance of T

• This is the first report of T-protein gene mutation in Oriental patients with nonketotic hyperglycinemia [1].

High impact information on T

• We previously discovered a cellular isoform of titin (originally named T-protein) colocalized with myosin II in the terminal web domain of the chicken intestinal epithelial cell brush border cytoskeleton (Eilertsen, K.J., and T.C.S. Keller. 1992. J. Cell Biol. 119:549-557) [2].
• One of these novel genes (Ch-TbxT) becomes restricted to the axial mesoderm lineage and is a potential candidate for complementing or extending Brachyury function in the anterior axis (formation of the head process, prechordal plate) [3].
• Therefore, Brachyury expression may act functionally upstream of cSox3 downregulation. cSox3 expression is also lost from non-neuronal ectoderm shortly after the neural plate becomes morphologically apparent. cSox2 expression increases dramatically in the central nervous system as neural ectoderm is established [4].
• In the area pellucida, both PN and HN transplants inhibited cell population growth while only PN caudalized the host axis and induced supernumerary primitive streaks expressing the mesoderm-specific gene Brachyury [5].
• A one-base deletion (183delC) and a missense mutation (D276H) in the T-protein gene from a Japanese family with nonketotic hyperglycinemia [1].

Chemical compound and disease context of T

• Two novel mutations in the gene encoding T-protein, a component of the glycine cleavage system, were identified in a Japanese family with nonketotic hyperglycinemia [1].

Anatomical context of T

• The mouse Brachyury gene (T) is required in notochord differentiation and posterior mesoderm formation during axial development [6].

References