Anti-TTLL4 antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

TTLL4 also known as Tubulin Tyrosine Ligase-Like Family Member 4 is an enzyme that catalyzes the polyglutamylation of proteins such as tubulin. It is part of the TTLL family of enzymes which add glutamate residues to substrate proteins. TTLL4 has a mass of approximately 141 kDa. This enzyme is mostly found in the brain and testis with higher expression levels in neuronal tissues. TTLL4 participates in the post-translational modification of microtubules impacting their dynamics and stability.

Biological function summary

This enzyme functions in the regulation of microtubule-associated processes. TTLL4 is not believed to be part of a known complex but its activity affects microtubule connections with cellular structures. Polyglutamylation impacts the interaction of microtubules with other proteins influencing cell division intracellular transport and ciliary movement. By modifying tubulin TTLL4 indirectly influences important cell functions through these microtubule-associated processes.

Pathways

TTLL4's activity connects to the regulation of the cytoskeleton and cilia formation. It plays a role in the proper functioning of neuronal cells by modulating microtubule stability through the addition of glutamate chains. TTLL4 works alongside proteins such as TPX2 involved in microtubule nucleation and others participating in cell cycle regulation. This enzyme also impacts pathways related to the stabilization of the axonal cytoskeleton critical for nerve cell function and signaling.

Associated diseases and disorders

Alteration in TTLL4's function links to neurodegenerative disorders and ciliopathies. Aberrant polyglutamylation may contribute to disorders like Alzheimer's disease by affecting tubulin stability and intracellular transport in association with proteins like tau. Additionally TTLL4 dysfunction may lead to faulty cilia formation and motility central to disorders like retinitis pigmentosa. Understanding its interaction with proteins in these diseases provides insight into potential therapeutic strategies.