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- W2900526774 abstract "Microtubule-associated end-binding protein 3 (EB3) accumulates asymmetrically at the tip-end of growing microtubules, providing a central platform for linking various cellular components. EB3 orchestrates microtubule dynamics and targeting, enabling diverse processes within neurons. Inositol 1, 4, 5-trisphosphate 3-kinase A (IP3K-A; also known as ITPKA) is a neuron-enriched protein that binds to microtubules by PKA-dependent manners. In this study, we found that IP3K-A binds to EB3 and their binding affinity is precisely regulated by protein kinase A (PKA)-dependent phosphorylation of IP3K-A at Ser119 (pSer119). We also revealed that the complex of IP3K-A and EB3 dissociates and reassociates rapidly during chemically induced LTP (cLTP) condition. This dynamic rearrangement of IP3K-A and EB3 complex will contribute remodeling of microtubule cytoskeleton allowing effective structural plasticity in response to synaptic stimulations." @default.
- W2900526774 created "2018-11-29" @default.
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- W2900526774 date "2019-01-01" @default.
- W2900526774 modified "2023-09-23" @default.
- W2900526774 title "PKA-dependent phosphorylation of IP3K-A at Ser119 regulates a binding affinity with EB3" @default.
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- W2900526774 doi "https://doi.org/10.1016/j.bbrc.2018.11.042" @default.
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