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Changdae Bae

Sungkyunkwan University · 生化学・遺伝学・分子生物学

研究室紹介

Professor Changdae Bae's research lab focuses on signal transduction mechanisms in the nervous system, with a particular emphasis on the roles of small GTPases, phospholipases, and mitogen-activated protein kinases (MAPKs) in neuronal signaling and plasticity. The lab investigates how these signaling molecules regulate cellular processes such as cytoskeletal reorganization, neurite outgrowth, and neuronal survival in response to stimuli like growth factors, seizures, and electroconvulsive shock. Key areas of interest include the regulation of phospholipase D by Rho family GTPases, the activation of MAPK pathways in excitotoxicity, and the post-translational modification of cytoskeletal regulators like moesin and PIX proteins. The lab employs a combination of biochemical, cell biological, and proteomic approaches to dissect these signaling networks in neuronal and cancer cells.

neuronal signalingRho GTPasesphospholipase DMAPK pathwayscytoskeletal regulation

Research Overview

Papers
50
Total Citations
782
Papers (5y)
8
Primary Field
生化学・遺伝学・分子生物学

Research Output Trend

Figures are computed from collected data and may differ slightly.

Publications per year (5y)
8total
2013
2014
2015
2016
2017
Citations per year (5y)
93total
20132014201520162017

Selected Papers

15
1
Article|81 citations·2000
Activation of JNK and p38 in rat hippocampus after kainic acid induced seizure
Song Hee Jeon, Yong Sik Kim, Chang‐Dae Bae, Joo-Bae Park
SJR Q1Experimental & Molecular MedicineOA

Kainic acid, an analogue of glutamate, causes limbic seizures and induces cell death in the rat brain. We examined the activation of MAPK family kinases; ERKs, JNKs and p38 kinase in rat hippocampus after KA treatment. Activation of all three kinases were observed at 30 min after the treatment, but, in contrary to ERK phosphorylation, which lasted up to 3 h, the phosphorylation of JNK and p38 returned to the basal level by 2 h. The phosphorylation of' upstream kinases for the MAPK family was dis

Cellular and Molecular NeuroscienceNeuroscience
2
Article|55 citations·2002
RhoA and Rho Kinase-dependent Phosphorylation of Moesin at Thr-558 in Hippocampal Neuronal Cells by Glutamate
Songhee Jeon, Sohee Kim, Jong‐Bae Park, Pann‐Ghill Suh, Yong Sik Kim, Chang‐Dae Bae, Joobae Park, Joobae Park, Joobae Park
SJR Q1Journal of Biological ChemistryOA

When we were studying phosphorylated proteins in the rat brain after electroconvulsive shock (ECS), we observed the rapid phosphorylation of a 75-kDa protein, which cross-reacted with the anti-phospho-p70 S6 kinase antibody. The phosphorylated protein was purified and identified as moesin, a member of the ezrin/radixin/moesin (ERM) family and a general cross-linker between cortical actin filaments and plasma membranes. The purified moesin from rat brain was phosphorylated at serine and threonine

Cellular and Molecular NeuroscienceNeuroscience
3
Article|52 citations·2004
Basic Fibroblast Growth Factor Stimulates Activation of Rac1 through a p85 βPIX Phosphorylation-dependent Pathway
Eun‐Young Shin, Kyung-Nam Woo, Chan‐Soo Lee, Seong-Hoe Koo, Young Gyu Kim, Won-Jai Kim, Chang‐Dae Bae, Soo‐Ik Chang, Eung‐Gook Kim
SJR Q1Journal of Biological ChemistryOA

In a previous study (Shin, E. Y., Shin, K. S., Lee, C. S., Woo, K. N., Quan, S. H., Soung, N. K., Kim, Y. G., Cha, C. I., Kim, S. R., Park, D., Bokoch, G. M., and Kim, E. G. (2002) J. Biol. Chem. 277, 44417-44430) we reported that phosphorylation of p85 betaPIX, a guanine nucleotide exchange factor (GEF) for Rac1/Cdc42, is a signal for translocation of the PIX complex to neuronal growth cones and is associated with basic fibroblast growth factor (bFGF)-induced neurite outgrowth. However, the iss

Molecular BiologyBiochemistry, Genetics and Molecular Biology
4
Article|40 citations·2007
Functional Importance of the Anaphase-Promoting Complex-Cdh1-Mediated Degradation of TMAP/CKAP2 in Regulation of Spindle Function and Cytokinesis
Kyung U. Hong, Young Soo Park, Yeon‐Sun Seong, Dongmin Kang, Chang‐Dae Bae, Joobae Park
SJR Q2Molecular and Cellular Biology

Cytoskeleton-associated protein 2 (CKAP2), also known as tumor-associated microtubule-associated protein (TMAP), is a novel microtubule-associated protein that is frequently upregulated in various malignances. However, its cellular functions remain unknown. A previous study has shown that its protein level begins to increase during G(1)/S and peaks at G(2)/M, after which it decreases abruptly. Ectopic overexpression of TMAP/CKAP2 induced microtubule bundling related to increased microtubule stab

Cell BiologyBiochemistry, Genetics and Molecular Biology
5
Article|35 citations·2009
TMAP/CKAP2 is essential for proper chromosome segregation
Kyung U. Hong, Eunhee Kim, Chang‐Dae Bae, Joobae Park
SJR Q1Cell CycleOA

Tumor-associated microtubule-associated protein (TMAP), also known as cytoskeleton associated protein 2 (CKAP2), is a novel mitotic spindle-associated protein which is frequently up-regulated in various malignances. However, its cellular functions remain unknown. Previous reports suggested that the cellular functions of TMAP/CKAP2 pertain to regulation of the dynamics and assembly of the mitotic spindle. To investigate its role in mitosis, we studied the effects of siRNA-mediated depletion of TM

Cell BiologyBiochemistry, Genetics and Molecular Biology
6
Article|31 citations·1998
Calpain inhibitors reduce the cornified cell envelope formation by inhibiting proteolytic processing of transglutaminase 1
Soo‐Youl Kim, Chang‐Dae Bae
SJR Q1Experimental & Molecular MedicineOA

Calpain I (mu-calpain) and II (m-calpain) are well known calcium-activated neutral cysteine proteases. Many reports have shown that activation of calpain is related to cataract formation, neuronal degeneration, blood clotting, ischemic injuries, muscular dystrophy and cornified cell envelope (CE) formation. Here, we report that insoluble CE formation was reduced after treatment with calpain I inhibitor (N-acetyl-leucyl-leucyl-norleucinal) on normal human epidermal keratinocytes (NHEK), whereas s

Cell BiologyBiochemistry, Genetics and Molecular Biology
7
Article|31 citations·2010
NGF-induced moesin phosphorylation is mediated by the PI3K, Rac1 and Akt and required for neurite formation in PC12 cells
Songhee Jeon, Jung‐Keug Park, Chang‐Dae Bae, Joobae Park
SJR Q2Neurochemistry International
Cell BiologyBiochemistry, Genetics and Molecular Biology
8
Article|28 citations·2014
Chromatin CKAP2, a New Proliferation Marker, as Independent Prognostic Indicator in Breast Cancer
Han‐Seong Kim, Jae‐Soo Koh, Yong‐Bock Choi∥, Jungsil Ro, Hyun‐Kyoung Kim, Mi‐Kyung Kim, Byung‐Ho Nam, Kyung‐Tae Kim, Vishal Chandra, Hyesil Seol, Woo-Chul Noh, Eun‐Kyu Kim
SJR Q1PLoS ONEOA

Chromatin CKAP2 is an independent prognostic marker for RFS in early-stage breast cancer, and could potentially replace the MAI in clinical evaluation of proliferation activity. Additionally, our study results suggest that the prognostic significance of proliferation activity differs among the various subgroups of breast cancer.

Cancer ResearchBiochemistry, Genetics and Molecular Biology
9
Article|26 citations·2010
Glutamate receptor‐mediated phosphorylation of ezrin/radixin/moesin proteins is implicated in filopodial protrusion of primary cultured hippocampal neuronal cells
Han‐Seop Kim, Chang‐Dae Bae, Joobae Park
SJR Q1Journal of Neurochemistry

Previously, we reported the phosphorylation of moesin induced by electroconvulsive shock in rat brain and by glutamate in immortalized rat hippocampal cells. However, the function of phosphorylated moesin in differentiated neurons is not well understood. In this study, we observed that glutamate induces phosphorylation of ezrin/radixin/moesin proteins (ERM) in cultured hippocampal cells and that phosphorylated ERM localizes at the newly formed filopodia of neurites. The glutamate-induced phospho

NeurologyMedicine
10
Article|24 citations·2006
A cytoskeleton-associated protein, TMAP/CKAP2, is involved in the proliferation of human foreskin fibroblasts
Sang‐Min Jeon, Bongkun Choi, Kyung U. Hong, Eun Hee Kim, Yeon‐Sun Seong, Chang‐Dae Bae, Joobae Park
SJR Q2Biochemical and Biophysical Research Communications
Pathology and Forensic MedicineMedicine
11
Article|24 citations·2008
Transient phosphorylation of tumor associated microtubule associated protein (TMAP)/cytoskeleton associated protein 2 (CKAP2) at Thr-596 during early phases of mitosis
Kyung U. Hong, Yong‐Bock Choi∥, Jung-Hwa Lee, Hyun‐Jun Kim, Hyerim Kwon, Yeon‐Sun Seong, Heung Tae Kim, Joobae Park, Chang‐Dae Bae, Kyeong‐Man Hong, Kyeong‐Man Hong, Kyeong‐Man Hong
SJR Q1Experimental & Molecular MedicineOA

Tumor associated microtubule associated protein (TMAP), also known as cytoskeleton associated protein 2 (CKAP2) is a mitotic spindle-associated protein whose expression is cell cycle-regulated and also frequently deregulated in cancer cells. Two monoclonal antibodies (mAbs) against TMAP/CKAP2 were produced: B-1-13 and D-12-3. Interestingly, the reactivity of mAb D-12-3 to TMAP/CKAP2 was markedly decreased specifically in mitotic cell lysate. The epitope mapping study showed that mAb D-12-3 recog

Cell BiologyBiochemistry, Genetics and Molecular Biology
12
Article|23 citations·2009
Cdk1-Cyclin B1-mediated Phosphorylation of Tumor-associated Microtubule-associated Protein/Cytoskeleton-associated Protein 2 in Mitosis
Kyung U. Hong, Hyunjun Kim, Hyo-Sil Kim, Yeon‐Sun Seong, Kyeong‐Man Hong, Chang‐Dae Bae, Joobae Park
SJR Q1Journal of Biological ChemistryOA

During mitosis, establishment of structurally and functionally sound bipolar spindles is necessary for maintaining the fidelity of chromosome segregation. Tumor-associated microtubule-associated protein (TMAP), also known as cytoskeleton-associated protein 2 (CKAP2), is a mitotic spindle-associated protein whose level is frequently up-regulated in various malignancies. Previous reports have suggested that TMAP is a potential regulator of mitotic spindle assembly and dynamics and that it is requi

Cell BiologyBiochemistry, Genetics and Molecular Biology
13
Article|21 citations·2005
Inhibition kinetics of mushroom tyrosinase by copper-chelating ammonium tetrathiomolybdate
Kyung‐Hee Park, Yong‐Doo Park, Jae-Rin Lee, Hwa-Sun Hahn, Sang-Jin Lee, Chang‐Dae Bae, Jun‐Mo Yang, Dong‐Eun Kim, Myong‐Joon Hahn
SJR Q2Biochimica et Biophysica Acta (BBA) - General Subjects
Cell BiologyBiochemistry, Genetics and Molecular Biology
14
Article|19 citations·2008
Transient phosphorylation of tumor associated microtubule associated protein (TMAP)/cytoskeleton associated protein 2 (CKAP2) at Thr-596 during early phases of mitosis
홍경욱, 최용복, Jung-Hwa Lee, Hyun-Jun Kim, Hye-Rim Kwon, 성연선, 김흥태, 박주배, 배창대, 홍경만
http://kmbase.medric.or.kr/Main.aspx?d=KMBASE&m=VIEW&i=0620920080400040377

Tumor associated microtubule associated protein (TMAP), also known as cytoskeleton associated protein 2 (CKAP2) is a mitotic spindle-associated protein whose expression is cell cycle-regulated and also frequently deregulated in cancer cells. Two monoclonal antibodies (mAbs) against TMAP/CKAP2 were produced: B-1-13 and D-12-3. Interestingly, the reactivity of mAb D-12-3 to TMAP/CKAP2 was markedly decreased specifically in mitotic cell lysate. The epitope mapping study showed that mAb D-12-3 recog

15
Article|19 citations·2017
CKAP2 (cytoskeleton-associated protein2) is a new prognostic marker in HER2-negative luminal type breast cancer
Sung Hoon Sim, Chang‐Dae Bae, Youngmi Kwon, Hai-Li Hwang, Shiv Poojan, Hyein Hong, Kyung‐Tae Kim, Seo-Hee Kang, Han‐Seong Kim, Tae Hyun Um, In Hae Park, Keun Seok Lee
SJR Q1PLoS ONEOA

The current study showed that CPCC but not Ki-67LI is an independent prognostic indicator in early breast cancer, more specifically in HER2-negative luminal breast cancer. The difference between two markers may be related to the lower background expression of CKAP2 in cancer cells.

Cancer ResearchBiochemistry, Genetics and Molecular Biology

Research Areas

Cell BiologyMolecular BiologyClinical BiochemistryCellular and Molecular NeuroscienceCancer ResearchPhysiology

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