Search Google Appliance

 
A B C D E F G H J K L M N O P R S T V W X Y Z

Please select the first letter of the last name you are looking for.

Margaret Stratton

Assistant Professor

The Stratton lab is focused on understanding the molecular components that allow you to form, maintain and recall a memory. CaMKII (calcium-calmodulin dependent protein kinase II) is the center of our focus. This dodecameric kinase complex has several fascinating biochemical and biophysical properties and is known to play a hallmark role in long-term memory. We have recently shown, for the first time, that CaMKII can exchange subunits between complexes, but only as a result of activation. Subunit exchange may play a role in extending the lifetime of active CaMKII, which could be necessary for memory potentiation.

The Stratton Lab is focused on the study of CaMKII in three major areas: frequency activation, subunit exchange, and downstream effectors. The overarching goal of the Stratton lab is to understand, at the molecular level, the protein regulation that drives synapse formation and maintenance. In order to understand the complexity that exists in our neural networks, we first need a detailed understanding of the proteins involved in memory formation at the level of their molecular structure, signaling properties and regulation. We aim to bridge the gap between information obtained at the animal level (e.g., transgenic mice) and information obtained at the molecular level (e.g., protein structure and regulation).

We use a variety of biochemical and biophysical techniques, complemented by in cellulo experiments and microscopy, to demonstrate the physiological relevance of these phenomena.

Current Research

We are currently pursuing the physiological relevance of subunit exchange in CaMKII as it pertains to functionality in a neuron. We continue to be curious about the molecular details of CaMKII assembly and subunit exchange. 
We are also pursuing proteins that are downstream of CaMKII. It is important to understand the regulation of all the pathways that eventually result in long term potentiation.

Learn more at sites.biochem.umass.edu/strattonlab/.

Academic Background

B.S., Biochemistry, Stonehill College
PhD, SUNY Upstate Medical University, Stewart Loh
Post doctoral fellow, UC Berkeley, John Kuriyan

1) M. Bhattacharyya*, M. M. Stratton*, Catherine Going*, Yongjian Huang, Ethan McSpadden, Anna Elleman, Pawel Burkhwat, Tiago Barros, Evan Williams and John Kuriyan, (2016) “Molecular Mechanism of activation-triggered subunit exchange in human CaMKII”, eLife, e13405.
2) M. M. Stratton*, I. H. Lee*, M. Bhattacharyya, S. M. Christensen, L. H. Chao, H. Schulman, J. T. Groves, J. Kuriyan, (2014) Activation-triggered subunit exchange between CaMKII holoenzymes facilitates the spread of kinase activity, eLife, 3:e01610. [PubMed]
3) M. M. Stratton, L. H. Chao, H. Schulman, J. Kuriyan, (2013) Structural studies on the regulation of Ca2+/calmodulin dependent protein kinase II, Current opinion in structural biology, 23, 292-301. [PubMed]
4) L. H. Chao, M. M. Stratton, I. H. Lee, J. Levitz, D. Mandell, T. Kortemme, H. Schulman, J. Kuriyan, (2011) A mechanism for tunable autoinhibition in the structure of a human Ca2+/calmodulin- dependent kinase II holoenzyme, Cell, 146, 732-745. [PubMed]
 
Contact Info

Biochemistry and Molecular Biology
1226 LGRT
710 North Pleasant Street
Amherst, MA 01003-9292

(413) 545-0631
mstratton@umass.edu

sites.biochem.umass.edu/strattonlab/