bp(GO:"microtubule polymerization")

Entity

Name

microtubule polymerization

Namespace

go

Namespace Version

20180921

Namespace URL

https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/go-names.belns

We concluded that FKBP52 inhibits the promotion of microtubule assembly by Tau. PubMed:20133804

These findings provide new insights into the regulation of microtubule assembly, since Ca2+/calmodulin inhibition of tubulin polymerization into microtubules could be mediated by the direct binding of calmodulin to tau, thus preventing the interaction of this latter protein with tubulin. PubMed:2123288

These findings provide new insights into the regulation of microtubule assembly, since Ca2+/calmodulin inhibition of tubulin polymerization into microtubules could be mediated by the direct binding of calmodulin to tau, thus preventing the interaction of this latter protein with tubulin. PubMed:2123288

Fluorescent imaging of these extracts revealed that wildtype FKBP51 promoted microtubule polymerization relative to extracts treated with buffer only (Fig 7A and S2). Conversely, neither mutant F130A FKBP51 nor FKBP52 stimulated microtubule formation. PubMed:20071522

We concluded that FKBP52 inhibits the promotion of microtubule assembly by Tau. PubMed:20133804

The data (Fig. 8B) shows that no significant difference in the extent of tubulin assembly could be observed with normal tau or tau incubated with CA. These results also indicate that once assembled, the microtubules remained stable to the same extent in the presence or in the absence of CA. PubMed:23531502

Because S199/S202/T205E, S396/S404E, 6-Phos and 7-Phos all demonstrated an AD-like shift in mobility as a result of phosphorylation-like changes, we conclude that they have the characteristics of hyperphosphorylated tau. These mutants will therefore be referred to as pseudo-hyperphosphorylated tau throughout the manuscript. On the basis of the observations that pseudohyperphosphorylated tau has decreased affinity for microtubules and reduced inducer-initiated rates of nucleation and polymerization, we propose that this combination could be the cause of the increased cytotoxicity of hyperphosphorylated tau in Alzheimer's disease and also explain the potentially beneficial role of tau polymerization and NFT formation. PubMed:19459590

Importantly, depletion of MARK1/2 reversed the inhibitory effect of DAPK on MT regrowth (Figure 5c, right panel). These results indicate that the DAPK–MARK signaling axis inhibits MT assembly and stability. PubMed:21311567

Importantly, depletion of MARK1/2 reversed the inhibitory effect of DAPK on MT regrowth (Figure 5c, right panel). These results indicate that the DAPK–MARK signaling axis inhibits MT assembly and stability. PubMed:21311567

Importantly, depletion of MARK1/2 reversed the inhibitory effect of DAPK on MT regrowth (Figure 5c, right panel). These results indicate that the DAPK–MARK signaling axis inhibits MT assembly and stability. PubMed:21311567

When overexpressed in rat hippocampal primary neurons, 14-3-3z causes an increase in Ser(262) phosphorylation, a decrease in the amount of microtubule-bound tau, a reduction in the amount of polymerized microtubules, as well as microtubule instability. Downregulation of synaptophysin in 14-3-3z overexpressing neurons was mitigated by inhibiting the proteosome, indicating that 14-3-3z promotes proteosomal degradation of synaptophysin. When 14-3-3z overexpressing neurons were treated with the microtubule stabilizing drug taxol, tau Ser(262) phosphorylation decreased and synaptophysin level was restored. PubMed:22941973

The excessive accumulation of phosphate groups in tau is associated with its altered capacity in promoting microtubule assembly and stability [4-6]. PubMed:22299660

Hyperphosphorylation of tau at the repeat domain reduces its microtubule binding, which may cause microtubule disassembly, leading to axonal transport deficits. PubMed:26631930

Tau aggregation decreases levels of soluble functional tau, which may result in microtubule disassembly as well PubMed:26631930

Owing to the additional repeat domain R2, 4R tau shows higher affinity for microtubules than does 3R tau, and is therefore more efficient at promoting microtubule assembly PubMed:26631930

Owing to the additional repeat domain R2, 4R tau shows higher affinity for microtubules than does 3R tau, and is therefore more efficient at promoting microtubule assembly PubMed:26631930

The truncation of tau at Asn368 has been observed in human AD brains and in a P301S mouse model of tauopathy, in which it leads to the generation of a tau1–368 fragment that is prone to aggregation and shows compromised microtubule-assembly activity, possibly contributing to tau aggregation and neurodegeneration. PubMed:26631930

Interestingly, the PSP-associated tau mutation A152T is localized far away from the repeat domain but still decreases the binding of tau to microtubules and therefore promotes microtubule assembly less efficiently PubMed:26631930

Cytoskeleton organization and dynamics depend on the fine control of microtubule assembly, which relies on the interaction of microtubules with a specific class of proteins known as microtubule-associated protein (MAP). PubMed:30061532

We concluded that FKBP52 inhibits the promotion of microtubule assembly by Tau. PubMed:20133804

Because S199/S202/T205E, S396/S404E, 6-Phos and 7-Phos all demonstrated an AD-like shift in mobility as a result of phosphorylation-like changes, we conclude that they have the characteristics of hyperphosphorylated tau. These mutants will therefore be referred to as pseudo-hyperphosphorylated tau throughout the manuscript. On the basis of the observations that pseudohyperphosphorylated tau has decreased affinity for microtubules and reduced inducer-initiated rates of nucleation and polymerization, we propose that this combination could be the cause of the increased cytotoxicity of hyperphosphorylated tau in Alzheimer's disease and also explain the potentially beneficial role of tau polymerization and NFT formation. PubMed:19459590

Cytoskeleton organization and dynamics depend on the fine control of microtubule assembly, which relies on the interaction of microtubules with a specific class of proteins known as microtubule-associated protein (MAP). PubMed:30061532