Hang Gao

Dr. Hang Gao


Research Focus & Metrics

Academic Career Length

6Years (2021-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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6 December 2021 in Molecular Plant Pathology
Verified
Journal Article
Open access
PDF file
QZQingfeng Zhou
Qingfeng Zhou
KMKang Ma
Kang Ma
HHHuanhuan Hu
Huanhuan Hu
XXXiaolong Xing
Xiaolong Xing
XHXuan Huang
Xuan Huang
HGHang Gao
Hang Gao
Extracellular vesicles (EVs) are rounded vesicles enclosed by a lipid bilayer membrane, released by eukaryotic cells and by bacteria. They carry various types of bioactive substances, including nucleic acids, proteins, and lipids. Depending on their cargo, EVs have a variety of well‐studied functions in mammalian systems, including cell‐to‐cell communication, cancer progression, and pathogenesis. In contrast, EVs in plant cells (which have rigid walls) have received very little research attention for many decades. Increasing evidence during the past decade indicates that both plant cells and plant pathogens are able to produce and secrete EVs, and that such EVs play key roles in plant–pathogen interactions. Plant EVs contains small RNAs (sRNAs) and defence‐related proteins, and may be taken up by pathogenic fungi, resulting in reduced virulence. On the other hand, EVs released by gram‐negative bacteria contain a wide variety of effectors and small molecules capable of activating plant immune responses via pattern‐recognition receptor‐ and BRI1‐ASSOCIATED RECEPTOR KINASE‐ and SUPPRESSOR OF BIR1‐mediated signalling pathways, and salicylic acid‐dependent and ‐independent processes. The roles of EVs in plant–pathogen interactions are summarized in this review, with emphasis on important molecules (sRNAs, proteins) present in plant EVs.

2 September 2022 in Molecular Plant Pathology
Verified
Journal Article
Open access
HGHang Gao
Hang Gao
KMKang Ma
Kang Ma
GJGuojie Ji
Guojie Ji
LPLiying Pan
Liying Pan
ZQZhou Qingfeng
Zhou Qingfeng
Nonspecific lipid transfer proteins (LTPs) are small, cysteine‐rich proteins that play numerous functional roles in plant growth and development, including cutin wax formation, pollen tube adhesion, cell expansion, seed development, germination, and adaptation to changing environmental conditions. LTPs contain eight conserved cysteine residues and a hydrophobic cavity that provides a wide variety of lipid‐binding specificities. As members of the pathogenesis‐related protein 14 family (PR14), many LTPs inhibit fungal or bacterial growth, and act as positive regulators in plant disease resistance. Over the past decade, these essential immunity‐related roles of LTPs in plant immune processes have been documented in a growing body of literature. In this review, we summarize the roles of LTPs in plant–pathogen interactions, emphasizing the underlying molecular mechanisms in plant immune responses and specific LTP functions.

30 December 2024 in Plant Cell Reports
Verified
Journal Article
Closed access
PDF file
WWWenjing Wang
Wenjing Wang
JZJunsong Zhang
Junsong Zhang
LPLiying Pan
Liying Pan
ZLZijia Liu
Zijia Liu
WYWeiwei Yi
Weiwei Yi
HGHang Gao
Hang Gao

1 February 2024 in Plant Science
Verified
Journal Article
Closed access
JZJunsong Zhang
Junsong Zhang
LPLiying Pan
Liying Pan
WXWenjie Xu
Wenjie Xu
HYHongchao Yang
Hongchao Yang
FHFuge He
Fuge He
HGHang Gao
Hang Gao

11 November 2021 in Frontiers in Plant Science
Verified
Journal Article
Open access
QZQingfeng Zhou
Qingfeng Zhou
QMQi Meng
Qi Meng
XTXiaomin Tan
Xiaomin Tan
WDWei Ding
Wei Ding
KMKang Ma
Kang Ma
HGHang Gao
Hang Gao
Systemic acquired resistance (SAR) in plants is a defense response that provides resistance against a wide range of pathogens at the whole-plant level following primary infection. Although the molecular mechanisms of SAR have been extensively studied in recent years, the role of phosphorylation that occurs in systemic leaves of SAR-induced plants is poorly understood. We used a data-independent acquisition (DIA) phosphoproteomics platform based on high-resolution mass spectrometry in an Arabidopsis thaliana model to identify phosphoproteins related to SAR establishment. A total of 8011 phosphorylation sites from 3234 proteins were identified in systemic leaves of Pseudomonas syringae pv. maculicola ES4326 (Psm ES4326) and mock locally inoculated plants. A total of 859 significantly changed phosphoproteins from 1119 significantly changed phosphopeptides were detected in systemic leaves of Psm ES4326 locally inoculated plants, including numerous transcription factors and kinases. A variety of defense response-related proteins were found to be differentially phosphorylated in systemic leaves of Psm ES4326 locally inoculated leaves, suggesting that these proteins may be functionally involved in SAR through phosphorylation or dephosphorylation. Significantly changed phosphoproteins were enriched mainly in categories related to response to abscisic acid, regulation of stomatal movement, plant–pathogen interaction, MAPK signaling pathway, purine metabolism, photosynthesis-antenna proteins, and flavonoid biosynthesis. A total of 28 proteins were regulated at both protein and phosphorylation levels during SAR. RT-qPCR analysis revealed that changes in phosphorylation levels of proteins during SAR did not result from changes in transcript abundance. This study provides comprehensive details of key phosphoproteins associated with SAR, which will facilitate further research on the molecular mechanisms of SAR.

20 October 2023 in PeerJ
Verified
Journal Article
Open access
PDF file
SJShuna Jiang
Shuna Jiang
LPLiying Pan
Liying Pan
QZQingfeng Zhou
Qingfeng Zhou
WXWenjie Xu
Wenjie Xu
FHFuge He
Fuge He
HGHang Gao
Hang Gao
Background: Plant-pathogen interactions occur in the apoplast comprising the cell wall matrix and the fluid in the extracellular space outside the plasma membrane. However, little is known regarding the contribution of the apoplastic proteome to systemic acquired resistance (SAR). Methods: Specifically, SAR was induced by inoculating plants with Pst DC3000 avrRps4. The apoplast washing fluid (AWF) was collected from the systemic leaves of the SAR-induced or mock-treated plants. A label free quantitative proteomic analysis was performed to identified the proteins related to SAR in AWF. Results: A total of 117 proteins were designated as differentially accumulated proteins (DAPs), including numerous pathogenesis-related proteins, kinases, glycosyl hydrolases, and redox-related proteins. Functional enrichment analyses shown that these DAPs were mainly enriched in carbohydrate metabolic process, cell wall organization, hydrogen peroxide catabolic process, and positive regulation of catalytic activity. Comparative analysis of proteome data indicated that these DAPs were selectively enriched in the apoplast during the induction of SAR. Conclusions: The findings of this study indicate the apoplastic proteome is involved in SAR. The data presented herein may be useful for future investigations on the molecular mechanism mediating the establishment of SAR.