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 | 2020-02-27T04:42:45Z | - |
dc.date.created | 2020-02-05 | - |
dc.date.issued | 2019-01-01 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/1992 | - |
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.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.subject | INOSITOL 1,4,5-TRISPHOSPHATE 3-KINASE | - |
dc.subject | PROTEIN-KINASE | - |
dc.subject | DENDRITIC SPINES | - |
dc.subject | EXPRESSION | - |
dc.subject | MORPHOLOGY | - |
dc.subject | ENDS | - |
dc.title | PKA-dependent phosphorylation of IP3K-A at Ser119 regulates a binding affinity with EB3 | - |
dc.type | Article | - |
dc.type.rims | ART | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000459089200008 | - |
dc.identifier.doi | 10.1016/j.bbrc.2018.11.042 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.508, no.1, pp.52 - 59 | - |
dc.identifier.scopusid | 2-s2.0-85056795396 | - |
dc.citation.endPage | 59 | - |
dc.citation.startPage | 52 | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 508 | - |
dc.citation.number | 1 | - |
dc.contributor.affiliatedAuthor | Cho, Yongsang | - |
dc.type.docType | Article | - |
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 | - |
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.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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