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| Type |
Oral Presentation |
| Area |
Oral Presentation of Young Analytical Chemists Ⅰ |
| Room No. |
303호 |
| Time |
THU 09:58-: |
| Code |
ANAL1.O-22 |
| Subject |
NMR Structural studies associated with the mechanism of Syndecan-4 Receptor |
| Authors |
김지선, 김용애*
한국외국어대학교 화학과, Korea
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| Abstract |
Syndecan-4 consists of heparan sulfate proteoglycans which are present on the surface of all cell types in humans. It provides a mechanical link among the extracellular matrix and the actin cytoskeleton via binding interactions of its cytoplasmic tail. Syndecan-4 interacts with various binding partners to increase wound healing, cell invasion and survival, activates focal adhesion and phosphorylates, and regulate cytoplasmic calcium concentration. In addition, the interaction of syndecan-4 with GFRs (growth factor receptors) is a very important factor in cancer progression and is particularly associated with resistance to treatment and therapy in breast cancer.
To get a better understanding of the mechanism and function of syndecan-4, it is crucial to investigate its three dimensional structure. Syndecan-4 comprises three major sections: extracellular (ecto-), transmembrane (TM) and cytoplasmic (Cyto-) domains. Syndecans have a very well conserved cytoplasmic region, but the V regions have a distinctive feature for each syndecan family member. The cytoplasmic domain of syndecan-4 consists of 28 amino acids and includes V domain. The binding of PIP2(phosphotidylinositol (4,5)-bisphosphate) at V domain of syndecan-4 causes the structural change of whole cytoplasmic domain of syndecan-4 and this leads binding and activation of PKC-α. Thus, the structural alteration of the transmembrane and cytoplasmic domains by binding with PKC-α and PIP2 regulates the function of the extracellular domain.
Here, we optimize recombinant production processes of syndecan-4 that contain wild type Syd4-TM (wtSyd4), mutant Syd4-TM(mSyd4) and Syd4-eTC(ecto-, TM, Cyto-). And its structure was investigated by solution/solid-state NMR spectroscopy.
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| E-mail |
cucu860@daum.net |
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119th General Meeting of the KCS