Polyglutamylation

Polyglutamylation
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Causes	Genetic mutation
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Polyglutamylation is a type of post-translational modification of proteins, where multiple glutamate residues are added to the gamma-carboxyl group of a glutamate side chain. This modification is catalyzed by a family of enzymes known as tubulin tyrosine ligase-like (TTLL) enzymes.

Function

Polyglutamylation plays a crucial role in the regulation of microtubule functions. It affects the interaction of microtubules with microtubule-associated proteins (MAPs) and motor proteins, thereby influencing cellular processes such as cell division, intracellular transport, and ciliary function.

Mechanism

The process of polyglutamylation involves the sequential addition of glutamate residues to the side chain of a glutamate residue in a protein. This is mediated by TTLL enzymes, which recognize specific protein domains and catalyze the addition of glutamate residues.

Biological Significance

Polyglutamylation is essential for the proper functioning of neurons and cilia. In neurons, it regulates the stability and dynamics of microtubules, which are critical for axon guidance and synaptic plasticity. In cilia, polyglutamylation is important for the assembly and maintenance of the axoneme, the core structure of cilia.

Clinical Implications

Defects in polyglutamylation have been linked to various neurological disorders and ciliopathies. Mutations in genes encoding TTLL enzymes can lead to neurodegenerative diseases and retinal degeneration.

Research

Ongoing research is focused on understanding the precise molecular mechanisms by which polyglutamylation affects microtubule functions and its implications in human diseases.

See also

• Post-translational modification
• Microtubule
• Ciliopathy

References

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External links

• [Polyglutamylation at Wikidata]