Membership Organizations

  • Arbor Free Clinic, Physician Recruitment and Staffing Coordinator

Education & Certifications

  • Bachelor of Science, University of California Los Angeles, Biochemistry (2011)
  • Bachelor of Science, University of California Los Angeles, GSB MBA Applied Natural Scienc (2011)


  • 2016 Autumn - PSYC 300A Psychiatry Core Clerkship
  • 2016 Summer - MED 314A Advanced Medicine Clerkship
  • 2015 Spring - NENS 301A Neurology Core Clerkship
  • 2015 Spring - OBGYN 300A Obstetrics and Gynecology Core Clerkship
  • 2015 Winter - DERM 300A Dermatology Clerkship
  • 2015 Winter - MED 300A Internal Medicine Core Clerkship
  • 2014 Autumn - PEDS 300A Pediatrics Core Clerkship
  • 2014 Autumn - SURG 300A Surgery Core Clerkship
  • 2014 Summer - MED 313A Ambulatory Medicine Core Clerkship
  • 2014 Summer - RAD 303A Specialty Clerkship in Diagnostic Radiology
  • 2014 Summer - SURG 300A Surgery Core Clerkship

Research & Scholarship

Current Research and Scholarly Interests

Scholarly Concentration: Clinical Research


All Publications

  • EFCAB7 and IQCE Regulate Hedgehog Signaling by Tethering the EVC-EVC2 Complex to the Base of Primary Cilia DEVELOPMENTAL CELL Pusapati, G. V., Hughes, C. E., Dorn, K. V., Zhang, D., Sugianto, P., Aravind, L., Rohatgi, R. 2014; 28 (5): 483-496


    The Hedgehog (Hh) pathway depends on primary cilia in vertebrates, but the signaling machinery within cilia remains incompletely defined. We report the identification of a complex between two ciliary proteins, EFCAB7 and IQCE, which positively regulates the Hh pathway. The EFCAB7-IQCE module anchors the EVC-EVC2 complex in a signaling microdomain at the base of cilia. EVC and EVC2 genes are mutated in Ellis van Creveld and Weyers syndromes, characterized by impaired Hh signaling in skeletal, cardiac, and orofacial tissues. EFCAB7 binds to a C-terminal disordered region in EVC2 that is deleted in Weyers patients. EFCAB7 depletion mimics the Weyers cellular phenotype-the mislocalization of EVC-EVC2 within cilia and impaired activation of the transcription factor GLI2. Evolutionary analysis suggests that emergence of these complexes might have been important for adaptation of an ancient organelle, the cilium, for an animal-specific signaling network.

    View details for DOI 10.1016/j.devcel.2014.01.021

    View details for Web of Science ID 000333405600004

    View details for PubMedID 24582806

  • High-Throughput Screening of Small Molecules Identifies Hepcidin Antagonists MOLECULAR PHARMACOLOGY Fung, E., Sugianto, P., Hsu, J., Damoiseaux, R., Ganz, T., Nemeth, E. 2013; 83 (3): 681-690


    Anemia of inflammation (AI) is common in patients with infection, autoimmune diseases, cancer, and chronic kidney disease. Unless the underlying condition can be reversed, treatment options are limited to erythropoiesis-stimulating agents with or without intravenous iron therapy, modalities that are not always effective and can cause serious adverse effects. Hepcidin, the iron regulatory hormone, has been identified as a pathogenic factor in the development of AI. To explore new therapeutic options for AI and other iron-related disorders caused by hepcidin excess, we developed a cell-based screen to identify hepcidin antagonists. Of the 70,000 small molecules in the library, we identified 14 compounds that antagonized the hepcidin effect on ferroportin. One of these was fursultiamine, a Food and Drug Administration (FDA)-approved thiamine derivative. Fursultiamine directly interfered with hepcidin binding to its receptor, ferroportin, by blocking ferroportin C326 thiol residue essential for hepcidin binding. Consequently, fursultiamine prevented hepcidin-induced ferroportin ubiquitination, endocytosis, and degradation in vitro and allowed continuous cellular iron export despite the presence of hepcidin, with IC(50) in the submicromolar range. Thiamine, the fursultiamine metabolite, and benfotiamine, another thiamine derivative, did not interfere with the effect of hepcidin on ferroportin. Other FDA-approved thiol-reactive compounds were at least 1000-fold less potent than fursultiamine in antagonizing hepcidin. In vivo, fursultiamine did not reproducibly antagonize the effect of hepcidin on serum iron, likely because of its rapid conversion to inactive metabolites. Fursultiamine is a unique antagonist of hepcidin in vitro that could serve as a template for the development of drug candidates that inhibit the hepcidin-ferroportin interaction.

    View details for DOI 10.1124/mol.112.083428

    View details for Web of Science ID 000315151900013

    View details for PubMedID 23292796

  • Hepcidin-Induced Endocytosis of Ferroportin Is Dependent on Ferroportin Ubiquitination CELL METABOLISM Qiao, B., Sugianto, P., Fung, E., del-Castillo-Rueda, A., Moran-Jimenez, M., Ganz, T., Nemeth, E. 2012; 15 (6): 918-924


    Ferroportin exports iron into plasma from absorptive enterocytes, erythrophagocytosing macrophages, and hepatic stores. The hormone hepcidin controls cellular iron export and plasma iron concentrations by binding to ferroportin and causing its internalization and degradation. We explored the mechanism of hepcidin-induced endocytosis of ferroportin, the key molecular event in systemic iron homeostasis. Hepcidin binding caused rapid ubiquitination of ferroportin in cell lines overexpressing ferroportin and in murine bone marrow-derived macrophages. No hepcidin-dependent ubiquitination was observed in C326S ferroportin mutant which does not bind hepcidin. Substitutions of lysines between residues 229 and 269 in the third cytoplasmic loop of ferroportin prevented hepcidin-dependent ubiquitination and endocytosis of ferroportin, and promoted cellular iron export even in the presence of hepcidin. The human ferroportin mutation K240E, previously associated with clinical iron overload, caused hepcidin resistance in vitro by interfering with ferroportin ubiquitination. Our study demonstrates that ubiquitination is the functionally relevant signal for hepcidin-induced ferroportin endocytosis.

    View details for DOI 10.1016/j.cmet.2012.03.018

    View details for Web of Science ID 000305502000016

    View details for PubMedID 22682227