While pursuing my MSc. degree in Biotechnology at the Tamil Nadu Agricultural University in India, I became fascinated with plant molecular genetics and biochemistry. I learned theoretical fundamentals in genetic engineering and decided to pursue these methodologies for making transgenic plants that could be beneficial for agriculture. Later, I was fortunate enough to be admitted to Washington State University for my doctoral research in the Poovaiah laboratory.

When I started at the Poovaiah lab, they had pioneered studies on calcium/calmodulin signaling in plants and discovered a calcium/calmodulin-dependent protein kinase (CCaMK) in lily plants while being engaged in actively characterizing its expression and biochemical properties. I took the challenge of elucidating the kinase’s function in plants by making a transgenic Arabidopsis plant that lacked CCaMK. Growing increasingly confident in my molecular biology skills, I began aggressively cloning an Arabidopsis homolog for CCaMK.  Fruitless months passed as I completed screening after screening, eventually enduring two and half years of no meaningful results. While still deeply passionate about my search for the Arabidopsis homolog, I realized that the clock was ticking for me to generate data capable of fueling a manuscript and meeting the requirements for my PhD. I was reading voraciously about calcium/calmodulin-dependent protein kinases from plants and animals when I came across a Science paper (Meyer et al., 1992) from the Schulman lab (Stanford University). This exciting paper described a novel biochemical property of calcium/calmodulin-dependent protein kinase in animals. The biochemical property, described as “calmodulin trapping,” is the enhanced affinity for calmodulin following autophosphorylation of the calcium/calmodulin dependent protein kinase.

Inspired and motivated, I immediately designed and executed experiments guided by the Meyer et al. paper to see whether CCaMK from lily might also show calmodulin trapping. To my surprise, CCaMK demonstrated autophosphorylation-dependent changes in affinity for calmodulin, resulting in my first first-author publication in the Journal of Biological Chemistry (2000) and giving me the additional benefit of peace of mind regarding my PhD. I carried out subsequent experiments and identified the phosphorylation site (Journal of Biological Chemistry, 2001) as well as autophosphorylation-induced structural changes (European Journal of Biochemistry, 2002) of CCaMK. My experiments on CCaMK exposed me to several new methodologies, including protein biochemistry, mass spectrometry, electron microscopy, and computational modeling, which I could apply to a diverse array of scientific disciplines in my future studies. More importantly, I became aware of the literature on mammalian kinases, especially neuronal calcium/calmodulin-dependent protein kinases. I was carried away by these readings, and together with my increasing expertise in molecular biology and biochemistry, I found myself changing my field of research to neurobiology. I wanted to know how human memory worked, fueled by my extensive readings in neuronal kinase literature.

Following my graduation, I was very fortunate to land a postdoctoral appointment in Eric Kandel’s laboratory at Columbia University – a dream come true for me – to study mechanisms of long-term memory storage. That was a transformative experience and led me to my current appointment at the world-class Scripps Research Institute as a Principal Investigator. Currently, my lab is actively pursuing molecular and cellular mechanisms underlying long-term memory storage and disorders of memory storage such as dementia and Alzheimer’s disease.

We thank Dr. Sathya Puthanveettil for his research and contribution to our blog. If you also work in the research field of plant biology or neurobiology you might be interested in  checking out our plant biology and neurobiology reagents.