Bio

Clinical Focus


  • Pediatric Pulmonary

Academic Appointments


Professional Education


  • Board Certification: Pediatric Pulmonary, American Board of Pediatrics (2010)
  • Board Certification: Pediatrics, American Board of Pediatrics (2007)
  • Fellowship:Lucile Packard Children's Hospital (2011) CA
  • Residency:Children's Hospital Oakland (2007) CA
  • Medical Education:Saint Louis University School of Medicine (2004) MO

Publications

Journal Articles


  • PML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/Chk2 NATURE CELL BIOLOGY Yang, S. T., Kuo, C., Bisi, J. E., Kim, M. K. 2002; 4 (11): 865-870

    Abstract

    The promyelocytic leukaemia (PML) gene is translocated in most acute promyelocytic leukaemias and encodes a tumour suppressor protein. PML is involved in multiple apoptotic pathways and is thought to be pivotal in gamma irradiation-induced apoptosis. The DNA damage checkpoint kinase hCds1/Chk2 is necessary for p53-dependent apoptosis after gamma irradiation. In addition, gamma irradiation-induced apoptosis also occurs through p53-independent mechanisms, although the molecular mechanism remains largely unknown. Here, we report that hCds1/Chk2 mediates gamma irradiation-induced apoptosis in a p53-independent manner through an ataxia telangiectasia-mutated (ATM)-hCds1/Chk2-PML pathway. Our results provide the first evidence of a functional relationship between PML and a checkpoint kinase in gamma irradiation-induced apoptosis.

    View details for DOI 10.1038/ncb869

    View details for Web of Science ID 000179137700015

    View details for PubMedID 12402044

  • Localization, dynamics, and protein interactions reveal distinct roles for ER and Golgi SNAREs JOURNAL OF CELL BIOLOGY Hay, J. C., Klumperman, J., Oorschot, V., Steegmaier, M., Kuo, C. S., Scheller, R. H. 1998; 141 (7): 1489-1502

    Abstract

    ER-to-Golgi transport, and perhaps intraGolgi transport involves a set of interacting soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins including syntaxin 5, GOS-28, membrin, rsec22b, and rbet1. By immunoelectron microscopy we find that rsec22b and rbet1 are enriched in COPII-coated vesicles that bud from the ER and presumably fuse with nearby vesicular tubular clusters (VTCs). However, all of the SNAREs were found on both COPII- and COPI-coated membranes, indicating that similar SNARE machinery directs both vesicle pathways. rsec22b and rbet1 do not appear beyond the first Golgi cisterna, whereas syntaxin 5 and membrin penetrate deeply into the Golgi stacks. Temperature shifts reveal that membrin, rsec22b, rbet1, and syntaxin 5 are present together on membranes that rapidly recycle between peripheral and Golgi-centric locations. GOS-28, on the other hand, maintains a fixed localization in the Golgi. By immunoprecipitation analysis, syntaxin 5 exists in at least two major subcomplexes: one containing syntaxin 5 (34-kD isoform) and GOS-28, and another containing syntaxin 5 (41- and 34-kD isoforms), membrin, rsec22b, and rbet1. Both subcomplexes appear to involve direct interactions of each SNARE with syntaxin 5. Our results indicate a central role for complexes among rbet1, rsec22b, membrin, and syntaxin 5 (34 and 41 kD) at two membrane fusion interfaces: the fusion of ER-derived vesicles with VTCs, and the assembly of VTCs to form cis-Golgi elements. The 34-kD syntaxin 5 isoform, membrin, and GOS-28 may function in intraGolgi transport.

    View details for Web of Science ID 000074605300002

    View details for PubMedID 9647643

  • Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells CELL Hay, J. C., Chao, D. S., Kuo, C. S., Scheller, R. H. 1997; 89 (1): 149-158

    Abstract

    The proposed cis-Golgi vesicle receptor syntaxin 5 was found in a complex with Golgi-associated SNARE of 28 kDa (GOS-28), rbet1, rsly1, and two novel proteins characterized herein: rat sec22b and membrin, both cytoplasmically oriented integral membrane proteins. The complex appears to recapitulate vesicle docking interactions of proteins originating from distinct compartments, since syntaxin 5, rbet1, and GOS-28 localize to Golgi membranes, whereas mouse sec22b and membrin accumulate in the endoplasmic reticulum. Protein interactions in the complex are dramatically rearranged by N-ethylmaleimide-sensitive factor. The complex consists of two or more subcomplexes with some members (rat sec22b and syntaxin 5) in common and others (rbet1 and GOS-28) mutually exclusively associated. We propose that these protein interactions determine vesicle docking/fusion fidelity between the endoplasmic reticulum and Golgi.

    View details for Web of Science ID A1997WR68500018

    View details for PubMedID 9094723

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