Jae U. Jung

Last updated
Jae U. Jung
Born1960 (age 6364)
Nationality South Korean
Alma materB.S. Seoul National University, Korea (1982)

M.S. Seoul National University, Korea(1984)

Ph.D. University of California-Davis(1989)
Awards2012 Ho-Am Prize in Medicine
Scientific career
Fields Medicine, Molecular Biology
Institutions Keck School of Medicine of USC
Korean name
Hangul
정재웅
Revised Romanization Jeong Jae-ung
McCune–Reischauer Jŏng Jaeung

Jae U. Jung is an expert in the molecular biology of herpes viruses and their gene products as they relate to cell biology, biochemistry and immunology. His research addresses several key biological features of virus-host interactions, with a focus on host immune responses to viruses, mechanisms by which viruses induce tumors, and the ability of viruses to establish lifelong infections. [1] [2]

Contents

Education

Known for

Publications

Awards and honors

Related Research Articles

<span class="mw-page-title-main">Autophagy</span> Cellular catabolic process in which cells digest parts of their own cytoplasm

Autophagy is the natural, conserved degradation of the cell that removes unnecessary or dysfunctional components through a lysosome-dependent regulated mechanism. It allows the orderly degradation and recycling of cellular components. Although initially characterized as a primordial degradation pathway induced to protect against starvation, it has become increasingly clear that autophagy also plays a major role in the homeostasis of non-starved cells. Defects in autophagy have been linked to various human diseases, including neurodegeneration and cancer, and interest in modulating autophagy as a potential treatment for these diseases has grown rapidly.

<span class="mw-page-title-main">Thapsigargin</span> Chemical compound

Thapsigargin is a non-competitive inhibitor of the sarco/endoplasmic reticulum Ca2+ ATPase (SERCA). Structurally, thapsigargin is classified as a guaianolide, and is extracted from a plant, Thapsia garganica. It is a tumor promoter in mammalian cells.

<span class="mw-page-title-main">Interleukin 29</span> Protein-coding gene in the species Homo sapiens

Interleukin-29 (IL-29) is a cytokine and it belongs to type III interferons group, also termed interferons λ (IFN-λ). IL-29 plays an important role in the immune response against pathogenes and especially against viruses by mechanisms similar to type I interferons, but targeting primarily cells of epithelial origin and hepatocytes.

<span class="mw-page-title-main">TANK-binding kinase 1</span> Protein-coding gene in the species Homo sapiens

TBK1 is an enzyme with kinase activity. Specifically, it is a serine / threonine protein kinase. It is encoded by the TBK1 gene in humans. This kinase is mainly known for its role in innate immunity antiviral response. However, TBK1 also regulates cell proliferation, apoptosis, autophagy, and anti-tumor immunity. Insufficient regulation of TBK1 activity leads to autoimmune, neurodegenerative diseases or tumorigenesis.

<span class="mw-page-title-main">BECN1</span> Protein-coding gene in the species Homo sapiens

Beclin-1 is a protein that in humans is encoded by the BECN1 gene. Beclin-1 is a mammalian ortholog of the yeast autophagy-related gene 6 (Atg6) and BEC-1 in the C. elegans nematode. This protein interacts with either BCL-2 or PI3k class III, playing a critical role in the regulation of both autophagy and cell death.

<span class="mw-page-title-main">ATG5</span> Protein-coding gene in the species Homo sapiens

Autophagy related 5 (ATG5) is a protein that, in humans, is encoded by the ATG5 gene located on Chromosome 6. It is an E3 ubi autophagic cell death. ATG5 is a key protein involved in the extension of the phagophoric membrane in autophagic vesicles. It is activated by ATG7 and forms a complex with ATG12 and ATG16L1. This complex is necessary for LC3-I conjugation to PE (phosphatidylethanolamine) to form LC3-II. ATG5 can also act as a pro-apoptotic molecule targeted to the mitochondria. Under low levels of DNA damage, ATG5 can translocate to the nucleus and interact with survivin.

<span class="mw-page-title-main">RALB</span> Protein-coding gene in the species Homo sapiens

Ras-related protein Ral-B (RalB) is a protein that in humans is encoded by the RALB gene on chromosome 2. This protein is one of two paralogs of the Ral protein, the other being RalA, and part of the Ras GTPase family. RalA functions as a molecular switch to activate a number of biological processes, majorly cell division and transport, via signaling pathways. Its biological role thus implicates it in many cancers.

<span class="mw-page-title-main">TRIM25</span> Protein-coding gene in the species Homo sapiens

Tripartite motif-containing protein 25 is a protein that in humans is encoded by the TRIM25 gene.

<span class="mw-page-title-main">VPS29</span> Protein-coding gene in the species Homo sapiens

VPS29 is a human gene coding for the vacuolar protein sorting protein Vps29, a component of the retromer complex.

<span class="mw-page-title-main">EBNA1BP2</span> Protein-coding gene in the species Homo sapiens

Probable rRNA-processing protein EBP2 is a protein that in humans is encoded by the EBNA1BP2 gene.

<span class="mw-page-title-main">IFITM1</span> Protein-coding gene in the species Homo sapiens

Interferon-induced transmembrane protein 1 is a protein that in humans is encoded by the IFITM1 gene. IFITM1 has also recently been designated CD225. This protein has several additional names: fragilis, IFI17 [interferon-induced protein 17], 9-27 [Interferon-inducible protein 9-27] and Leu13.

<span class="mw-page-title-main">AP4M1</span> Protein-coding gene in the species Homo sapiens

AP-4 complex subunit mu-1 is a protein that in humans is encoded by the AP4M1 gene.

Mitophagy is the selective degradation of mitochondria by autophagy. It often occurs to defective mitochondria following damage or stress. The process of mitophagy was first described over a hundred years ago by Margaret Reed Lewis and Warren Harmon Lewis. Ashford and Porter used electron microscopy to observe mitochondrial fragments in liver lysosomes by 1962, and a 1977 report suggested that "mitochondria develop functional alterations which would activate autophagy." The term "mitophagy" was in use by 1998.

AuTophaGy related 1 (Atg1) is a 101.7kDa serine/threonine kinase in S.cerevisiae, encoded by the gene ATG1. It is essential for the initial building of the autophagosome and Cvt vesicles. In a non-kinase role it is - through complex formation with Atg13 and Atg17 - directly controlled by the TOR kinase, a sensor for nutrient availability.

<span class="mw-page-title-main">Autophagy-related protein 13</span> Protein-coding gene in the species Homo sapiens

Autophagy-related protein 13 also known as ATG13 is a protein that in humans is encoded by the KIAA0652 gene.

In molecular biology, autophagy related 3 (Atg3) is the E2 enzyme for the LC3 lipidation process. It is essential for autophagy. The super protein complex, the Atg16L complex, consists of multiple Atg12-Atg5 conjugates. Atg16L has an E3-like role in the LC3 lipidation reaction. The activated intermediate, LC3-Atg3 (E2), is recruited to the site where the lipidation takes place.

RIG-I-like receptors are a type of intracellular pattern recognition receptor involved in the recognition of viruses by the innate immune system. RIG-I is the best characterized receptor within the RIG-I like receptor (RLR) family. Together with MDA5 and LGP2, this family of cytoplasmic pattern recognition receptors (PRRs) are sentinels for intracellular viral RNA that is a product of viral infection. The RLR receptors provide frontline defence against viral infections in most tissues.

Chaperone-assisted selective autophagy is a cellular process for the selective, ubiquitin-dependent degradation of chaperone-bound proteins in lysosomes.

<span class="mw-page-title-main">Stimulator of interferon genes</span> Protein-coding gene in the species Homo sapiens

Stimulator of interferon genes (STING), also known as transmembrane protein 173 (TMEM173) and MPYS/MITA/ERIS is a protein that in humans is encoded by the STING1 gene.

Francis "Frank" Vincent Chisari is a physician, experimental pathologist, virologist, and immunologist, known for his research on virus-host interactions of hepatitis B and hepatitis C.

References

  1. "Jae U. Jung | USC Global Conference 2013". Globalconference2013.usc.edu. Retrieved 2013-11-29.
  2. Liang, C; Lee, JS; Inn, KS; Gack, MU; Li, Q; Roberts, EA; Vergne, I; Deretic, V; Feng, P; Akazawa, C; Jung, JU (Jul 2008). "Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking". Nat Cell Biol. 10 (7): 776–87. doi:10.1038/ncb1740. PMC   2878716 . PMID   18552835.