权益分类	功能权益	普通用户	{{item.name}}会员
{{category.name}}	{{benefitItem.name}}

Bridging the Glycome and Proteome with Chemical Biology

用化学生物学连接糖组和蛋白质组

基本信息

批准号：
10798880
负责人：
Mia L Huang
金额：
$ 8.65万
依托单位：
SCRIPPS RESEARCH INSTITUTE, THE
依托单位国家：
美国
项目类别：
财政年份：
2021
资助国家：
美国
起止时间：
2021-06-01 至 2026-04-30
项目状态：
未结题

项目摘要

PROJECT SUMMARY During pregnancy, the proper development of the placenta is essential to maintain the health of the fetus and mother; however, we still do not have a clear understanding of how certain components of the placenta normally form. We are interested in how the synctitiotrophoblast barrier is formed through cellular fusion, and to understand this process, we will focus on the proteins presented on the outside of the barrier called cell surface proteins (CSPs). CSPs are regulators of cell-cell interactions and help cells respond to their environment, making them biologically important and relevant drug targets. However, CSPs are challenging to study, because they are in low abundance and are covered with sugar molecules called glycans. These glycans are highly variable structures that cannot be predicted, requiring experimental evidence to ascertain their composition. One of the most important functions of these glycans is to interact with glycan-binding proteins (GBPs). GBPs bind to glycans on the cell surface, resulting in downstream changes to cell behavior. GBPs, like galectin-3, have been shown to be necessary for normal fetal development and placental cell fusion, but discovering their mechanism of action is challenging, as the weak and dynamic interactions between glycans and GBPs are not easy to capture. To overcome these limitations, we have developed two new techniques that allow us to label and identify CSPs and galectin-3 interactors in live cells. We will apply these methods to a model of placental cell fusion to understand the factors that lead to successful barrier formation. Once critical CSPs and galectin-3 interactors are uncovered, we will perform genetic and biochemical experiments to determine their functions in detail. We will map the signaling pathways within the cell that allow for fusion, as well as the composition of glycans that allow for GBP interactions.

项目总结

项目成果

期刊论文数量（15）

专著数量（0）

科研奖励数量（0）

会议论文数量（0）

专利数量（0）

Proximity labeling technologies to illuminate glycan-protein interactions.

邻近标记技术阐明聚糖-蛋白质相互作用。

DOI：
10.1016/j.cbpa.2022.102233
发表时间：
2023
期刊：
Current opinion in chemical biology
影响因子：
7.8
作者：
Reeves,AbigailE;Huang,MiaL
通讯作者：
Huang,MiaL

Surfaceome Profiling Identifies Basigin-Chaperoned Protein Clients.

表面组分析可识别 Basigin 陪伴的蛋白质客户。

DOI：
10.1002/cbic.202300073
发表时间：
2023
期刊：
Chembiochem : a European journal of chemical biology
影响因子：
0
作者：
Vilen,Zak;Joeh,Eugene;Lee,Elizabeth;Huang,MiaL
通讯作者：
Huang,MiaL

Chemoproteomic mapping of human milk oligosaccharide (HMO) interactions in cells.

DOI：
10.1039/d2cb00176d
发表时间：
2022-11-30
期刊：
RSC CHEMICAL BIOLOGY
影响因子：
4.1
作者：
Hassan, Abdullah A.;Wozniak, Jacob M.;Vilen, Zak;Li, Weichao;Jadhav, Appaso;Parker, Christopher G.;Huang, Mia L.
通讯作者：
Huang, Mia L.

Mapping glycan-mediated galectin-3 interactions by live cell proximity labeling.

DOI：
10.1073/pnas.2009206117
发表时间：
2020-11-03
期刊：
Proceedings of the National Academy of Sciences of the United States of America
影响因子：
11.1
作者：
Joeh E;O'Leary T;Li W;Hawkins R;Hung JR;Parker CG;Huang ML
通讯作者：
Huang ML

Chemical editing of proteoglycan architecture.

DOI：
10.1038/s41589-022-01023-5
发表时间：
2022-06
期刊：
NATURE CHEMICAL BIOLOGY
影响因子：
14.8
作者：
O'Leary, Timothy R.;Critcher, Meg;Stephenson, Tesia N.;Yang, Xueyi;Hassan, Abdullah A.;Bartfield, Noah M.;Hawkins, Richard;Huang, Mia L.
通讯作者：
Huang, Mia L.