Bio

Born and raised in Hawaii. Moved to Seattle, WA to study biology and biochemistry at the University of Washington. After graduating, I moved to Bethesda, MD to work at the NIH as an IRTA fellow. Currently in the Shen Lab studying microtubule biology in C. elegans neurons

Education & Certifications

  • B.S., University of Washington, Biochemistry (2017)
  • B.S., University of Washington, Biology (2017)

Contact

Additional Info

  • Mail Code: 5020
  • SUNet ID(s):
    dkawano

All Publications

  • Dephosphorylation of Y228 and Y217 and phosphorylation of Y335 in p120 catenin activate convergent extension during zebrafish gastrulation. Developmental dynamics : an official publication of the American Association of Anatomists Shan, B., Horton, E. C., Xu, S. C., Huntington, K. E., Kawano, D. K., Mendoza, C. L., Lin, L., Stafford, C. M., Allen, E. D., Huang, J., Nakahara, H., Greenstein, L. E., Hille, M. B. 2022

    Abstract

    BACKGROUND: The cadherin-associated protein p120 catenin regulates convergent extension through interactions with cadherin proteins, Cdc42, and Rac1, as we previously showed in zebrafish (Danio rerio). Phosphorylation of p120 catenin changes the nature of its activity in vitro but is virtually unexplored in embryos. We used our previously developed antisense RNA splice-site morpholino targeted to endogenous p120 catenin-delta1 to cause defects in axis elongation probing the functions of three p120 catenin tyrosine-phosphorylation sites in gastrulating zebrafish embryos.RESULTS: The morpholino-induced defects were rescued by co-injections with mouse p120 catenin-delta1-3A mRNAs mutated at residues Y228 and Y217 to a non-phosphorylatable phenylalanine (F) or mutated at residue Y335 to a phosphomimetic glutamic acid (E). Co-injection of the complementary mutations Y228E, Y217E, or Y335F mRNAs partially rescued embryos whereas dual mutation to Y228E-Y217E blocked rescue. Immunopurification showed Y228F mutant proteins preferentially interacted with Rac1, potentially promoting cell migration. In contrast, the phosphomimetic Y228E preferentially interacted with E-cadherin increasing adhesion. Both Y228F and Y335F strongly bind VAV2.CONCLUSIONS: p120 catenin serves dual roles during gastrulation of zebrafish. Phosphorylation and dephosphorylation of tyrosine residues Y217, Y228, and Y335 precisely balance cell adhesion and cell migration to facilitate somite compaction and axis elongation. This article is protected by copyright. All rights reserved.

    View details for DOI 10.1002/dvdy.524

    View details for PubMedID 35996230

  • Infrequent Fluctuations in Temperature and Salinity May Enhance Feeding in Pisaster ochraceus (Asteroidea) but Not in Dendraster excentricus (Echinoidea) Larvae BIOLOGICAL BULLETIN George, S. B., Navarro, E., Kawano, D. 2021

    View details for DOI 10.1086/716054

    View details for Web of Science ID 000683459000001