Inositol 1,4,5-trisphosphate 3-kinase A is a novel microtubule-associated protein: PKA-dependent phosphoregulation of microtubule binding affinity

Dongmin Lee, Hyun Woo Lee, Soontaek Hong, Byung Il Choi, Hyun Wook Kim, Seung Baek Han, Il Hwan Kim, Jin Young Bae, Yong Chul Bae, Im Joo Rhyu, Woong Sun, Hyun Kim

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Inositol 1,4,5-trisphosphate 3-kinase A (IP3K-A) is a brain specific and F-actin-binding protein. Werecently demonstrated that IP 3K-A modulates a structural reorganization of dendritic spines through F-actin remodeling, which is required for synaptic plasticity and memory formation in brain. However, detailed functions of IP3K-A and its regulatory mechanisms involved in the neuronal cytoskeletal dynamics still remain unknown. In the present study, we identified tubulin as a candidate of IP3K-A-binding protein through proteomic screening. By various in vitro and in vivo approaches, we demonstrated that IP3K-A was a novel microtubule-associated protein (MAP), and the N terminus of IP3K-A was a critical region for direct binding to tubulin in dendritic shaft of hippocampal neurons. Moreover, PKA phosphorylated Ser-119 within IP 3K-A, leading to a significant reduction of microtubule binding affinity. These results suggest that PKA-dependent phosphorylation and microtubule binding of IP3K-A are involved in its regulatory mechanism for activity-dependent neuronal events such as local calcium signaling and its synaptic targeting.

Original languageEnglish
Pages (from-to)15981-15995
Number of pages15
JournalJournal of Biological Chemistry
Volume287
Issue number19
DOIs
Publication statusPublished - 2012 May 4

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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