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PKA-dependent phosphorylation of IP3K-A at Ser119 regulates a binding affinity with EB3

Authors
Mo, Seo JungCho, YongsangChoi, Byung-ilLee, DongminKim, Hyun
Issue Date
Jan-2019
Publisher
Academic Press
Keywords
IP3K-A; EB3; Cytoskeleton; PKA; Phosphorylation; Neuron
Citation
Biochemical and Biophysical Research Communications, v.508, no.1, pp 52 - 59
Pages
8
Indexed
SCI
SCIE
SCOPUS
Journal Title
Biochemical and Biophysical Research Communications
Volume
508
Number
1
Start Page
52
End Page
59
URI
https://scholarworks.korea.ac.kr/kumedicine/handle/2020.sw.kumedicine/2499
DOI
10.1016/j.bbrc.2018.11.042
ISSN
0006-291X
1090-2104
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. (C) 2018 Elsevier Inc. All rights reserved.
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