the enzyyme catalyzes tubulin polyglutamylation with high preference to beta-tubulin in vitro. When expressed in HEK293T cells, TTLL7 demonstrates specificity for beta-tubulin and not for alpha-tubulin or nucleosome assembly protein 1
pH 7.0, 30°C, at a 600fold higher concentration compared with the ATP concentration, almost completely inhibits the enzyme. Competitive inhibition for ATP. Noncompetitive inhibitor for glutamate and tubulin
consistent with having a role in the growth of MAP2-positive neurites, TTLL7 accumulates within a MAP2-enriched somatodendritic portion of superior cervical ganglion, as does polyglutamylated beta-tubulin
knockdown of TTLL7 in a primary culture of superior cervical ganglion neurons causes a loss of polyglutamylated beta-tubulin. Short interference RNA-mediated knockdown of TTLL7 represses nerve growth factor-stimulated MAP (microtubule-associated protein) 2-positive neurite growth in PC12 cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
structure of TTLL7 bound to the microtubule. Enzyme displays a tripartite microtubule recognition strategy and uses its core to engage the disordered anionic tails of alpha- and beta-tubulin, and a flexible cationic domain to bind the microtubule and position itself for beta-tail modification