IndraLab

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TPX2 activates AURKA. 10 / 130
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sparser
"TPX2 activates AurA through conformational changes and triggers protection of the T288 residue from dephosphorylation by PP1 phosphatase ( xref ; xref )."

reach
"We have shown that the addition of TPX2 (1-43) increases the catalytic efficiency of AurA."

reach
"The AURKA activator TPX2, is overexpressed in many cancers, and through AURKA binding, allosteric modulation, and protection of the T288 phosphorylation site from dephosphorylation, TPX2 increases AURKA levels and maintains its active state, augmenting AURKA oncogenic effects in the cell ."

eidos
"Another pathway with a role in the mitosis control is called AURKA Activation by TPX2 ."
| DOI

reach
"Tpx2 further activates AurA by stabilizing a water mediated allosteric network that links the C-helix to the active site through an unusual polar residue in the regulatory spine."

sparser
"For organelle localization the major processes affected are organelle localization (logP = − 3.8), microtubule-based processes (logP = − 3.5), loss of Nlp from mitotic centrosomes (logP = − 3.4), AURKA activation by TPX2 (logP = − 3.4), centrosome maturation (logP = − 3.2), regulation of PLK1 activity at G2/M transition (logP = − 3.1), and recruitment of NuMa to mitotic centrosome (logP = − 2.9) ( Supplementary Table xref )."

sparser
"Overexpression of TPX2 activated AURKA and caused resistance ( xref ) whereas expression of other reported AURKA activators did not ( xref )."

sparser
"This view is consistent with recent work showing that AurA can be activated independently by Tpx2 or by phosphorylation on T288 by up to ∼100-fold in vitro [ xref , xref , xref , xref ]."

sparser
"The ability of the PKA-like water network to support activation of AurA by Tpx2 suggests a conserved role for the water network in kinase function."

reach
"The contrasting ability of AurA to be independently activated by phosphorylation or Tpx2 is dependent upon a unique active-site water network that strengthens the regulatory spine of the kinase relative to that of the AGC kinases."