Regulation of microtubules Sample Clauses

Regulation of microtubules. The regulation of microtubules are not completely understood but is thought to be due to both post-translational modifications of tubulin and other regulatory pathways involved in the polymerization and depolymerization states of microtubules. Cellular factors called microtubule associated proteins (MAPs) have been discovered to interact with microtubules and function to regulate tubulin assembly (124). Additionally, research studies show that expression of α- and β-tubulin isoforms could also affect microtubule dynamics. Taken together, these factors combine help to control the dynamic nature of microtubules within the cell. MAPs are mainly known to regulate microtubule polymerization. These proteins bind to microtubules and stabilize them. Unlike the assembly of microtubules, this binding does not depend on the GTP/GDP state of microtubules but rather is electrostatic and involves the acidic C-terminal domain of tubulin subunits. The classical stabilizing MAPs include MAP1, MAP2, MAP4, and tau. They are negatively regulated by phosphorylation which reduces the affinity of these proteins with the microtubule network. There are also a few destabilizing factors which reduce the net assembly of microtubules and increase microtubule turnover. Katanin functions as a severing factor at the ends of microtubules, generating new ends lacking the protective GTP gap, leading to massive disassembly. Depolymerizing kinesins bind to both ends of microtubules and forces protofilament peeling. Though this leads mainly to negative regulation of microtubule development, it is required for the formation and the dynamic nature of microtubules. Isoforms of tubulin Tubulin is encoded by a multigene family of proteins. The tubulin superfamily includes alpha, beta, gamma, delta, epsilon, and zeta. The cellular function of epsilon and zeta is still unknown. Gamma-tubulin is approximately 30% identical to the most common isoforms, alpha and beta. Distinct isotypes of α- and β-tubulin exists and are highly conserved, being the most variable in the last 10-15 amino acids of the C- terminus. The variability primarily affects the association of accessory proteins and not necessarily the polymerization of microtubules. In total, at least six isoforms of alpha and eight isoforms of beta are present in mammals. There is evidence that tubulin isotypes exhibit some tissue specificity since they are differentially expressed. In most instances, the isoforms seems functionally interchangeable...
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