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

Seo Jung Mo, Yongsang Cho, Byung il Choi, Dongmin Lee, Hyun Kim

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)52-59
Number of pages8
JournalBiochemical and biophysical research communications
Issue number1
Publication statusPublished - 2019 Jan 1


  • Cytoskeleton
  • EB3
  • IP3K-A
  • Neuron
  • PKA
  • Phosphorylation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'PKA-dependent phosphorylation of IP3K-A at Ser119 regulates a binding affinity with EB3'. Together they form a unique fingerprint.

Cite this