Bio

Education & Certifications


  • Master of Arts, Stanford University, REES-MA (2012)
  • Bachelor of Science, Stanford University, SLAV-MIN (2011)
  • Bachelor of Science, Stanford University, BIO-BSH (2011)

Clerkships


  • 2016 Autumn - FAMMED 301A Family Medicine Core Clerkship
  • 2016 Autumn - MED 313A Ambulatory Medicine Core Clerkship
  • 2016 Spring - MED 314A Advanced Medicine Clerkship
  • 2016 Spring - OBGYN 300A Obstetrics and Gynecology Core Clerkship
  • 2016 Summer - EMED 308A Bedside Ultrasound Clerkship
  • 2016 Summer - NENS 308A Adult Neurology Clerkship
  • 2016 Winter - MED 300A Internal Medicine Core Clerkship
  • 2016 Winter - RAD 301A Diagnostic Radiology and Nuclear Medicine Clerkship
  • 2015 Autumn - NENS 301A Neurology Core Clerkship
  • 2015 Autumn - PEDS 300A Pediatrics Core Clerkship
  • 2015 Summer - PSYC 300A Psychiatry Core Clerkship
  • 2015 Summer - SURG 300A Surgery Core Clerkship

Service, Volunteer and Community Work


  • Student Manager, Pacific Free Clinic (3/28/2010 - 3/23/2011)

    Location

    Stanford, CA

Publications

All Publications


  • A multi-protein receptor-ligand complex underlies combinatorial dendrite guidance choices in C. elegans. eLife Zou, W., Shen, A., Dong, X., Tugizova, M., Xiang, Y. K., Shen, K. 2016; 5

    Abstract

    Ligand receptor interactions instruct axon guidance during development. How dendrites are guided to specific targets is less understood. The C. elegans PVD sensory neuron innervates muscle-skin interface with its elaborate dendritic branches. Here, we found that LECT-2, the ortholog of leukocyte cell-derived chemotaxin-2 (LECT2), is secreted from the muscles and required for muscle innervation by PVD. Mosaic analyses showed that LECT-2 acted locally to guide the growth of terminal branches. Ectopic expression of LECT-2 from seam cells is sufficient to redirect the PVD dendrites onto seam cells. LECT-2 functions in a multi-protein receptor-ligand complex that also contains two transmembrane ligands on the skin, SAX-7/L1CAM and MNR-1, and the neuronal transmembrane receptor DMA-1. LECT-2 greatly enhances the binding between SAX-7, MNR-1 and DMA-1. The activation of DMA-1 strictly requires all three ligands, which establishes a combinatorial code to precisely target and pattern dendritic arbors.

    View details for DOI 10.7554/eLife.18345

    View details for PubMedID 27705746

  • MTM-6, a Phosphoinositide Phosphatase, is Required to Promote Synapse Formation in Caenorhabditis elegans PLOS ONE Ericson, V. R., Spilker, K. A., Tugizova, M. S., Shen, K. 2014; 9 (12)
  • Caenorhabditis elegans Muscleblind homolog mbl-1 functions in neurons to regulate synapse formation NEURAL DEVELOPMENT Spilker, K. A., Wang, G. J., Tugizova, M. S., Shen, K. 2012; 7

    Abstract

    The sequestration of Muscleblind splicing regulators results in myotonic dystrophy. Previous work on Muscleblind has largely focused on its roles in muscle development and maintenance due to the skeletal and cardiac muscle degeneration phenotype observed in individuals with the disorder. However, a number of reported nervous system defects suggest that Muscleblind proteins function in other tissues as well.We have identified a mutation in the Caenorhabditis elegans homolog of Muscleblind, mbl-1, that is required for proper formation of neuromuscular junction (NMJ) synapses. mbl-1 mutants exhibit selective loss of the most distal NMJ synapses in a C. elegans motorneuron, DA9, visualized using the vesicle-associated protein RAB-3, as well as the active zone proteins SYD-2/liprin-? and UNC-10/Rim. The proximal NMJs appear to have normal pre- and postsynaptic specializations. Surprisingly, expressing a mbl-1 transgene in the presynaptic neuron is sufficient to rescue the synaptic defect, while muscle expression has no effect. Consistent with this result, mbl-1 is also expressed in neurons.Based on these results, we conclude that in addition to its functions in muscle, the Muscleblind splice regulators also function in neurons to regulate synapse formation.

    View details for DOI 10.1186/1749-8104-7-7

    View details for Web of Science ID 000304541600001

    View details for PubMedID 22314215

Footer Links:

Stanford Medicine Resources: