BSc in Psychology and Mathematics, University of Auckland, New Zealand, 1992-1995
MSc in Medical Science, University of Auckland, New Zealand, 1995-1997
PhD in Neuroscience, University of Auckland, New Zealand, 1997-1999
Fellow, Human Genetics, Massachusetts General Hospital/Harvard Med School, 2000-2003
Fellow, Auditory Neuroscience, Massachusetts Eye & Ear Infirmary/Harvard Med School, 2003-2005
Fellow, Neuroscience, Stanford University School of Medicine, 2005-2007
Dr. Cuajungco is a Neuroscientist from New Zealand. He earned his Ph.D. in Neuroscience at the University of Auckland, where he worked very productively on zinc metabolism and toxicity in the brain. As a pre-doctoral researcher at Harvard Medical School, he pursued a link between metal toxicity and Alzheimer’s disease. He then undertook post-doctoral work at Harvard, and acquired molecular biology expertise in studying a rare sensory neuropathy known as familial dysautonomia. His work evolved to problems in the sensory system and joined another Harvard laboratory to study molecules and nerve cells involved in hearing. His laboratory subsequently moved to Stanford School of Medicine, and his project led to his current interest in a family of membrane channels known as the Transient Receptor Potential (TRP) ion channels. The TRP ion channels mediate cell response to sensory stimuli such as taste, sight, sound, pain, or temperature. Their dysfunction results in many human diseases.
Transient Receptor Potential (TRP) ion channels and lysosomes in human health and neurodegenerative diseases
Lysosomes are important cell organelles involved in the breakdown of membrane proteins and other molecules. These intracellular vesicles have been implicated in many neurodegenerative disorders such as Alzheimer’s disease, Parkinson’s disease, and Mucolipidosis type IV. The lysosomal membrane contains a diverse number of receptor and ion channel proteins that mediate its normal function. Some of these proteins are also involved in protein trafficking through processes known as endocytosis and exocytosis. It is thus not surprising that dysfunction of these proteins result in human pathological conditions.
The Cuajungco lab is interested in the roles that specific lysosomal membrane proteins and ion channels play during normal and pathological states. Our investigations involve collaborations from various disciplines within CSUF and other renowned institutions. We use both prokaryotic and eukaryotic cell culture models, as well as molecular and cellular biology methods to accomplish our research goals. One of our projects use membrane-based yeast two-hybrid genetic screens to identify protein-protein interactors for TRP channels found in lysosomes. Subsequently, we aim to characterize the functional significance of identified membrane protein interactors for the TRP channels using biochemical and microscopy techniques. Another aspect of our research is to study the relationships between lysosomes and metal transport or storage using fluorescence imaging and spectroscopy. Finally, we use RNA interference to target lysosomal membrane proteins, and analyze functional defects, as well as uncover any unknown signaling pathways involved in cellular endocytosis and exocytosis events.
Grimm, C., Jörs, S., Saldanha, S.A., Obukhov, A.G., Pan, B., Oshima, K., Cuajungco, M.P., Chase, P., Hodder, P., and Heller, S. (2010). Small molecule activators of TRPML3. Chemistry and Biology, 17, 135-148. NCBI link
Samie M.A.*, Grimm C., Evans J.E.#, Curcio-Morelli, C., Heller, S., Slaugenhaupt, S.A. and Cuajungco, M.P. (2009) The tissue-specific expression of TRPML2 (MCOLN-2) gene is influenced by the presence of TRPML1. Pflügers Archiv – European Journal of Physiology, 459, 79-91 NCBI link (http://www.ncbi.nlm.nih.gov/pubmed/19763610). #Undergraduate student, *Graduate student.
Cuajungco, M.P. and Samie, M.A.* (2008) The varitint-waddler mouse phenotypes and the TRPML3 mutation: cause and consequence. Pflügers Archiv – European Journal of Physiology, 457, 463-473. *Graduate student. NCBI link (http://www.ncbi.nlm.nih.gov/pubmed/18504603?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum)
D`hoedt, D., Owsianik, G., Prenen, J., Cuajungco, M.P., Grimm, C., Heller, S., Voets, T. and Nilius, B. (2008) Stimulus-specific Modulation of the Cation Channel TRPV4 by PACSIN 3. Journal of Biological Chemistry, 283, 6272-6280. NCBI link (http://www.ncbi.nlm.nih.gov/pubmed/18174177?ordinalpos=2&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum)
Grimm, C., Cuajungco, M.P., van Aken, A.F.J., Schnee, M., Jors, S., Kros, C.J., Ricci, A.J. and Heller, S. (2007) A helix-breaking mutation in TRPML3 leads to constitutive activity underlying deafness in the varitint-waddler mouse. Proceedings of the National Academy of Sciences USA, 104, 19583-19588. NCBI link (http://www.ncbi.nlm.nih.gov/pubmed/18048323?ordinalpos=3&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum)
Cuajungco, M.P., Grimm, C., Oshima, K., D`Hoedt, D., Mensenkamp, A. R., Bindels, R. J., Nilius, B., Plomann, M., and Heller, S. (2006) PACSINs bind to the TRPV4 cation channel: PACSIN 3 modulates the subcellular localization of TRPV4. Journal of Biological Chemistry, 281, 18753-18762. NCBI link (http://www.ncbi.nlm.nih.gov/pubmed/16627472?ordinalpos=5&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum)
Faculty Recognition for Creative and Scholarly Activity, California State University Fullerton, April 2010
Undergraduate Student Award Recipients in the Cuajungco Laboratory
Jonathan Eichelsdoerfer Jeffrey A. Evans
Jeffrey A. Evans