Tubulin Folding Cofactor

Tubulin Folding Cofactor

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About TBC / Tubulin Folding Cofactor:

Microtubules are made of two main structural components- alpha-tubulin and beta-tubulin. However, a group of cofactors is also vital for assembly component formation of the tubulin molecule in vitro. While the vitro form is just an emerging role for the cofactors, their primary biological function in vivo is unclear.

TBC Mechanism
From a biological analysis in the mammalian system, tubulins with cofactors consist of various chaperonin subunits.
Tubulin folding cofactor B and A capture alpha and beta-tubulins after being released from the chaperonin complex, replacing them with cofactors E and D. the pathways converge to form a complex with four molecules. TBC is conserved from humans to yeast. For instance, budding yeast has homologs of various cofactors apart from cofactor C, which is found in mutants, genomes, and consequent genes.

Tubulin Folding Cofactor Functions
Tubulin folding cofactors are responsible for the availability of the tubulin subunits and microtubule stability in eukaryotes. According to recent Arabidopsis mutant experiments, there is another cellular function of tubulin folding cofactors.
Microtubules have dynamic properties controlled by various microtubules-binding proteins to stabilize, cluster, depolymerize and nucleate MT. Tubulin cofactors also regulate the synthesis of tubulin subunits, the formation of dimers, and the stability of microtubules. Tubulin folding cofactors are also essential in plant development.
Initially, tubulin folding cofactor activity was discovered through vertebrate proteins. Recent studies have shown that tubulin folding cofactors are vital in plant morphogenesis. However, there is no evidence to show their role in multicellular development.