PKA-dependent phosphorylation of IP3K-A at Ser119 regulates a binding affinity with EB3
DC Field | Value | Language |
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dc.contributor.author | Mo, Seo Jung | - |
dc.contributor.author | Cho, Yongsang | - |
dc.contributor.author | Choi, Byung-il | - |
dc.contributor.author | Lee, Dongmin | - |
dc.contributor.author | Kim, Hyun | - |
dc.date.available | 2020-11-02T06:44:25Z | - |
dc.date.issued | 2019-01 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.issn | 1090-2104 | - |
dc.identifier.uri | https://scholarworks.korea.ac.kr/kumedicine/handle/2020.sw.kumedicine/2499 | - |
dc.description.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. | - |
dc.format.extent | 8 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | Academic Press | - |
dc.title | PKA-dependent phosphorylation of IP3K-A at Ser119 regulates a binding affinity with EB3 | - |
dc.type | Article | - |
dc.publisher.location | 미국 | - |
dc.identifier.doi | 10.1016/j.bbrc.2018.11.042 | - |
dc.identifier.scopusid | 2-s2.0-85056795396 | - |
dc.identifier.wosid | 000459089200008 | - |
dc.identifier.bibliographicCitation | Biochemical and Biophysical Research Communications, v.508, no.1, pp 52 - 59 | - |
dc.citation.title | Biochemical and Biophysical Research Communications | - |
dc.citation.volume | 508 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 52 | - |
dc.citation.endPage | 59 | - |
dc.type.docType | Article | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | sci | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.subject.keywordPlus | INOSITOL 1,4,5-TRISPHOSPHATE 3-KINASE | - |
dc.subject.keywordPlus | PROTEIN-KINASE | - |
dc.subject.keywordPlus | DENDRITIC SPINES | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | MORPHOLOGY | - |
dc.subject.keywordPlus | ENDS | - |
dc.subject.keywordAuthor | IP3K-A | - |
dc.subject.keywordAuthor | EB3 | - |
dc.subject.keywordAuthor | Cytoskeleton | - |
dc.subject.keywordAuthor | PKA | - |
dc.subject.keywordAuthor | Phosphorylation | - |
dc.subject.keywordAuthor | Neuron | - |
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