About

Hakeoung Hannah Lee is an Assistant Professor at the UVA School of Education and Human Development. Her scholarship centers on empowering K–12 students, especially multicultural and multilingual learners from marginalized communities, by developing and deploying AI-enhanced multimodal learning analytics approaches in STEM learning contexts. Grounded in sociocultural perspectives, her work focuses on designing and deploying AI-enhanced multimodal video analysis systems and embedding learning analytics in context, with particular attention to responsible and ethical AI design. Her research aims to reveal the diverse and complex nature of student participation, which is often oversimplified or misrepresented by existing AI tools that rely solely on text-based or single-modality data. Lee positions herself as a scholar bridging the fields of learning sciences and learning analytics, with an interdisciplinary and multilingual background spanning K-12 education, statistics and programming, learning sciences, and STEM education. Her work has been published in various peer-reviewed journals and proceedings, and she has received numerous awards, including three national government awards for distinguished achievements in science, ICT, education, and equity, such as the Talent Award of Korea conferred by the Minister of the Korean Ministry of Education. In addition to her research, Lee is a founding member and Director of Research for the nonprofit Society of Technology for Education and Learning Analytics, where she promotes responsible and impactful use of technology in education with practitioners and policymakers.

Research topics

• Genetics
• Cell biology
• Biology
• Cancer research
• Chemistry
• Biochemistry
• Neuroscience

Selected publications

• Data from A small-molecule compound identified through a cell-based screening inhibits JAK/STAT pathway signaling in human cancer cells

  2023-03-31

  preprintOpen access

  <div>Abstract<p>Inappropriate activation of JAK/STAT signaling occurs with high frequency in human cancers and is associated with cancer cell survival and proliferation. Therefore, the development of pharmacologic STAT signaling inhibitors has therapeutic potential in the treatment of human cancers. Here, we report 2-[(3,5-bis-trifluoromethyl-phenyl)-hydroxy-methyl]-1-(4-nitro-phenylamino)-6-phenyl-1,2,4a,7a-tetrahydro-pyrrolo[3,4-<i>b</i>]-pyridine-5,7-dione (AUH-6-96) as a novel small-molecule inhibitor of JAK/STAT signaling that we initially identified through a cell-based high-throughput screening using cultured <i>Drosophila</i> cells. Treatment of <i>Drosophila</i> cells with AUH-6-96 resulted in a reduction of Unpaired-induced transcriptional activity and tyrosine phosphorylation of STAT92E, the sole <i>Drosophila</i> STAT homologue. In human cancer cell lines, AUH-6-96 inhibited both constitutive and interleukin-6-induced STAT3 phosphorylation. Specifically, in Hodgkin lymphoma L540 cells, treatment with AUH-6-96 resulted in reduced levels of tyrosine phosphorylated STAT3 and of the STAT3 downstream target gene <i>SOCS3</i> in a dose- and time-dependent manner. In addition, AUH-6-96-treated L540 cells showed decreased expression of persistently activated JAK3, suggesting that AUH-6-96 inhibits the JAK/STAT pathway signaling in L540 cells by affecting JAK3 activity and subsequently blocking STAT3 signaling. Importantly, AUH-6-96 selectively affected cell viability only of cancer cells harboring aberrant JAK/STAT signaling. In support of the specificity of AUH-6-96 for inhibition of JAK/STAT signaling, treatment with AUH-6-96 decreased cancer cell survival by inducing programmed cell death by down-regulating the expression of STAT3 downstream target antiapoptotic genes, such as Bcl-xL. In summary, this study shows that AUH-6-96 is a novel small-molecule inhibitor of JAK/STAT signaling and may have therapeutic potential in the treatment of human cancers harboring aberrant JAK/STAT signaling. [Mol Cancer Ther 2008;7(9):2672–80]</p></div>

  PublisherDOI

• Supplementary Fig. S3 from A small-molecule compound identified through a cell-based screening inhibits JAK/STAT pathway signaling in human cancer cells

  2023

  • Cancer research
  • Cell biology
  • Chemistry

  Supplementary Fig. S3 from A small-molecule compound identified through a cell-based screening inhibits JAK/STAT pathway signaling in human cancer cells

  PublisherOA PDFDOI

• Gcap14 is a microtubule plus-end-tracking protein coordinating microtubule–actin crosstalk during neurodevelopment

  Proceedings of the National Academy of Sciences · 2023 · 9 citations

  • Cell biology
  • Biology
  • Neuroscience

  knockout mice exhibited impaired cortical lamination. Gcap14 deficiency resulted in defective neuronal migration. Moreover, nuclear distribution element nudE-like 1 (Ndel1), an interacting partner of Gcap14, effectively corrected the downregulation of microtubule dynamics and the defects in neuronal migration caused by Gcap14 deficiency. Finally, we found that the Gcap14-Ndel1 complex participates in the functional link between microtubule and actin filament, thereby regulating their crosstalks in the growth cones of cortical neurons. Taken together, we propose that the Gcap14-Ndel1 complex is fundamental for cytoskeletal remodeling during neurodevelopmental processes such as neuronal processes elongation and neuronal migration.

  PublisherDOI

• Supplementary Fig. S1 from A small-molecule compound identified through a cell-based screening inhibits JAK/STAT pathway signaling in human cancer cells

  2023-03-31

  preprintOpen access

  Supplementary Fig. S1 from A small-molecule compound identified through a cell-based screening inhibits JAK/STAT pathway signaling in human cancer cells

  PublisherOA PDFDOI

• Supplementary Fig. S2 from A small-molecule compound identified through a cell-based screening inhibits JAK/STAT pathway signaling in human cancer cells

  2023-03-31

  preprintOpen access

  Supplementary Fig. S2 from A small-molecule compound identified through a cell-based screening inhibits JAK/STAT pathway signaling in human cancer cells

  PublisherOA PDFDOI

• Supplementary Fig. S1 from A small-molecule compound identified through a cell-based screening inhibits JAK/STAT pathway signaling in human cancer cells

  2023-03-31

  preprintOpen access

  Supplementary Fig. S1 from A small-molecule compound identified through a cell-based screening inhibits JAK/STAT pathway signaling in human cancer cells

  PublisherDOI

• Data from A small-molecule compound identified through a cell-based screening inhibits JAK/STAT pathway signaling in human cancer cells

  2023-03-31

  preprintOpen access

  <div>Abstract<p>Inappropriate activation of JAK/STAT signaling occurs with high frequency in human cancers and is associated with cancer cell survival and proliferation. Therefore, the development of pharmacologic STAT signaling inhibitors has therapeutic potential in the treatment of human cancers. Here, we report 2-[(3,5-bis-trifluoromethyl-phenyl)-hydroxy-methyl]-1-(4-nitro-phenylamino)-6-phenyl-1,2,4a,7a-tetrahydro-pyrrolo[3,4-<i>b</i>]-pyridine-5,7-dione (AUH-6-96) as a novel small-molecule inhibitor of JAK/STAT signaling that we initially identified through a cell-based high-throughput screening using cultured <i>Drosophila</i> cells. Treatment of <i>Drosophila</i> cells with AUH-6-96 resulted in a reduction of Unpaired-induced transcriptional activity and tyrosine phosphorylation of STAT92E, the sole <i>Drosophila</i> STAT homologue. In human cancer cell lines, AUH-6-96 inhibited both constitutive and interleukin-6-induced STAT3 phosphorylation. Specifically, in Hodgkin lymphoma L540 cells, treatment with AUH-6-96 resulted in reduced levels of tyrosine phosphorylated STAT3 and of the STAT3 downstream target gene <i>SOCS3</i> in a dose- and time-dependent manner. In addition, AUH-6-96-treated L540 cells showed decreased expression of persistently activated JAK3, suggesting that AUH-6-96 inhibits the JAK/STAT pathway signaling in L540 cells by affecting JAK3 activity and subsequently blocking STAT3 signaling. Importantly, AUH-6-96 selectively affected cell viability only of cancer cells harboring aberrant JAK/STAT signaling. In support of the specificity of AUH-6-96 for inhibition of JAK/STAT signaling, treatment with AUH-6-96 decreased cancer cell survival by inducing programmed cell death by down-regulating the expression of STAT3 downstream target antiapoptotic genes, such as Bcl-xL. In summary, this study shows that AUH-6-96 is a novel small-molecule inhibitor of JAK/STAT signaling and may have therapeutic potential in the treatment of human cancers harboring aberrant JAK/STAT signaling. [Mol Cancer Ther 2008;7(9):2672–80]</p></div>

  PublisherDOI

• Supplementary Fig. S2 from A small-molecule compound identified through a cell-based screening inhibits JAK/STAT pathway signaling in human cancer cells

  2023-03-31

  preprintOpen access

  Supplementary Fig. S2 from A small-molecule compound identified through a cell-based screening inhibits JAK/STAT pathway signaling in human cancer cells

  PublisherDOI

• Supplementary Fig. S3 from A small-molecule compound identified through a cell-based screening inhibits JAK/STAT pathway signaling in human cancer cells

  2023

  • Cancer research
  • Cell biology
  • Chemistry

  Supplementary Fig. S3 from A small-molecule compound identified through a cell-based screening inhibits JAK/STAT pathway signaling in human cancer cells

  PublisherDOI

• GRAMD1B regulates cell migration in breast cancer cells through JAK/STAT and Akt signaling

  Scientific Reports · 2018-06-18 · 54 citations

  articleOpen access

  Dysregulated JAK/STAT signaling has been implicated in breast cancer metastasis, which is associated with high relapse risks. However, mechanisms underlying JAK/STAT signaling-mediated breast tumorigenesis are poorly understood. Here, we showed that GRAMD1B expression is upregulated on IL-6 but downregulated upon treatment with the JAK2 inhibitor AG490 in the breast cancer MDA-MB-231 cells. Notably, Gramd1b knockdown caused morphological changes of the cells, characterized by the formation of membrane ruffling and protrusions, implicating its role in cell migration. Consistently, GRAMD1B inhibition significantly enhanced cell migration, with an increase in the levels of the Rho family of GTPases. We also found that Gramd1b knockdown-mediated pro-migratory phenotype is associated with JAK2/STAT3 and Akt activation, and that JAK2 or Akt inhibition efficiently suppresses the phenotype. Interestingly, AG490 dose-dependently increased p-Akt levels, and our epistasis analysis suggested that the effect of JAK/STAT inhibition on p-Akt is via the regulation of GRAMD1B expression. Taken together, our results suggest that GRAMD1B is a key signaling molecule that functions to inhibit cell migration in breast cancer by negating both JAK/STAT and Akt signaling, providing the foundation for its development as a novel biomarker in breast cancer.

  PublisherOA PDFDOI

Frequent coauthors

• Gyeong‐Hun Baeg

  New York Medical College

  11 shared

• Erika A. Bach

  New York University

  10 shared

• Agnieszka Ulaczyk‐Lesanko

  University of Alberta

  9 shared

• Qianxu Guo

  Loxo Oncology at Lilly (United States)

  9 shared

• Byung Hak Kim

  New York Medical College

  9 shared

• Changhong Yin

  East Carolina University

  9 shared

• Claudio Sandoval

  9 shared

• Dennis G. Hall

  9 shared

Awards & honors

• Three national government awards for distinguished achieveme…
• Talent Award of Korea, conferred by the Minister of the Kore…