PKA-dependent phosphorylation of IP3K-A at Ser119 regulates a binding affinity with EB3
- Authors
- Mo, Seo Jung; Cho, Yongsang; Choi, Byung-il; Lee, Dongmin; Kim, Hyun
- Issue Date
- 1-Jan-2019
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- IP3K-A; EB3; Cytoskeleton; PKA; Phosphorylation; Neuron
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.508, no.1, pp.52 - 59
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 508
- Number
- 1
- Start Page
- 52
- End Page
- 59
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/68364
- DOI
- 10.1016/j.bbrc.2018.11.042
- ISSN
- 0006-291X
- 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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Collections - Graduate School > Department of Biomedical Sciences > 1. Journal Articles
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