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

doi:10.1016/j.bbrc.2018.11.042

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 journal › Article › peer-review

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.

Original language	English
Journal	Biochemical and Biophysical Research Communications
DOIs	https://doi.org/10.1016/j.bbrc.2018.11.042
Publication status	Accepted/In press - 2018 Jan 1

Keywords

Cytoskeleton
EB3
IP3K-A
Neuron
Phosphorylation
PKA

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "PKA-dependent phosphorylation of IP3K-A at Ser119 regulates a binding affinity with EB3",

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.",

keywords = "Cytoskeleton, EB3, IP3K-A, Neuron, Phosphorylation, PKA",

author = "Mo, {Seo Jung} and Yongsang Cho and Choi, {Byung il} and Dongmin Lee and Hyun Kim",

year = "2018",

month = jan,

day = "1",

doi = "10.1016/j.bbrc.2018.11.042",

language = "English",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

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T1 - PKA-dependent phosphorylation of IP3K-A at Ser119 regulates a binding affinity with EB3

AU - Mo, Seo Jung

AU - Cho, Yongsang

AU - Choi, Byung il

AU - Lee, Dongmin

AU - Kim, Hyun

PY - 2018/1/1

Y1 - 2018/1/1

N2 - 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.

AB - 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.

KW - Cytoskeleton

KW - EB3

KW - IP3K-A

KW - Neuron

KW - Phosphorylation

KW - PKA

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DO - 10.1016/j.bbrc.2018.11.042

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JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

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

Abstract

Keywords

ASJC Scopus subject areas

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