Denghao Zheng

ORCID: 0000-0003-4058-2511
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About
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Research Areas
  • Autophagy in Disease and Therapy
  • Multiple Myeloma Research and Treatments
  • Cellular transport and secretion
  • Immune Cell Function and Interaction
  • Immunotherapy and Immune Responses
  • Hematopoietic Stem Cell Transplantation
  • Cancer Cells and Metastasis
  • Epigenetics and DNA Methylation
  • Lysosomal Storage Disorders Research
  • Nonmelanoma Skin Cancer Studies
  • Genital Health and Disease
  • Hedgehog Signaling Pathway Studies
  • Protein Degradation and Inhibitors
  • Ubiquitin and proteasome pathways
  • Cancer and Skin Lesions
  • HER2/EGFR in Cancer Research
  • Urological Disorders and Treatments
  • Neonatal Respiratory Health Research
  • Signaling Pathways in Disease
  • Galectins and Cancer Biology
  • Urologic and reproductive health conditions

Shanghai Jiao Tong University
2019-2024

Tongren Hospital
2020-2024

Indiana University School of Medicine
2019

Novartis (Switzerland)
2011

Autophagy is crucial for degrading and recycling cellular components. Fusion between autophagosomes lysosomes pivotal, directing autophagic cargo to degradation. This process driven by STX17-SNAP29-VAMP8 STX7-SNAP29-YKT6 in mammalian cells. However, the interaction STX17 YKT6 its significance remain be revealed. In this study, we challenge notion that function independently autophagosome-lysosome fusion. YKT6, through SNARE domain, forms a complex with SNAP29 on autophagosomes, enhancing...

10.1016/j.celrep.2024.113760 article EN cc-by-nc-nd Cell Reports 2024-02-01

The multi-subunit homotypic fusion and vacuole protein sorting (HOPS) membrane-tethering complex is required for autophagosome-lysosome in mammals, yet reconstituting the mammalian HOPS remains a challenge. Here we propose "hook-up" model assembly, which requires two sub-complexes docking on membranes via membrane-associated Rabs. We identify Rab39A as key small GTPase that recruits onto autophagic vesicles. Proper pairing with Rab2 enables assembly between proteoliposomes its tethering...

10.1038/s41467-023-42003-0 article EN cc-by Nature Communications 2023-10-11

Abstract Although multiple myeloma (MM) responds well to immunotherapeutic treatment, certain portions of MM are still unresponsive or relapse after immunotherapy. Other immune molecules needed for the immunotherapy MM. Here, we revealed that leukocyte immunoglobulin-like receptor B4 (LILRB4) was highly expressed in cell lines and patient samples expression LILRB4 adversely correlated with overall survival patients. Knockdown efficiently delayed growth cells both vitro vivo. Mechanistically,...

10.1038/s41419-024-06883-4 article EN cc-by Cell Death and Disease 2024-07-18

<title>Abstract</title> Although multiple myeloma (MM) responds well to immunotherapeutic treatment, certain portions of MM are still unresponsive or relapse after immunotherapy. Other immune molecules needed for the immunotherapy MM. Here, we revealed that leukocyte immunoglobulin-like receptor B4 (LILRB4) was highly expressed in cell lines and patient samples expression LILRB4 adversely correlated with overall survival patients. Knockdown efficiently delayed growth cells both vitro vivo....

10.21203/rs.3.rs-3885016/v1 preprint EN cc-by Research Square (Research Square) 2024-02-20
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