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 | |
| Publication status | Accepted/In press - 2018 Jan 1 |
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Keywords
- Cytoskeleton
- EB3
- IP3K-A
- Neuron
- Phosphorylation
- PKA
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
PKA-dependent phosphorylation of IP3K-A at Ser119 regulates a binding affinity with EB3. / Mo, Seo Jung; Cho, Yongsang; Choi, Byung il; Lee, Dongmin; Kim, Hyun.
In: Biochemical and Biophysical Research Communications, 01.01.2018.Research output: Contribution to journal › Article
}
TY - JOUR
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
UR - http://www.scopus.com/inward/record.url?scp=85056795396&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85056795396&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2018.11.042
DO - 10.1016/j.bbrc.2018.11.042
M3 - Article
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
ER -