Margaret Stratton
Assistant Professor
Office
LGRT 1226
(413) 545-0631
Fax
(413) 545-3291
Focus
Understanding the molecular mechanism of memory formation by dissecting the function and structural regulation of key proteins in this process. A major focus is CaMKII and its substrates/ binding partners, because CaMKII required for long-term memory formation.
Background and Training

PhD: SUNY Upstate Medical University
Postdoctoral training: University of California, Berkeley

Research Summary

https://www.strattonlab.com/

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.

Publications

G. Ardestani, M. C. West, T. J. Maresca, R. A. Fissore, M. M. Stratton, (2019) “FRET-based sensor for CaMKII activity (FRESCA): A useful tool for assessing CaMKII activity in response to Ca2+ oscillations in live cells” jbc.RA119.009235. [JBC]

M. S. Eriksen, O. Nikolanienko, E. I. Hallin, S. Grødem, H. J. Bustad, M. I. Flydal, R. O’Connell, T. Hosokawa, D. Lascu, S. Akerkar, J. Cuéllar, J. J. Chambers, G. Muruganandam, R. Loris, T. Kanhema, Y. Hayashi, M. M. Stratton, J. M. Valpuesta, P. Kursula, A. Martinez, C. R. Bramham, (2019) “Molecular determinants of Arc oligomerization and formation of virus-like capsids” bioRxiv 667956. [bioRxiv]

T. Saneyoshi, H. Matsuno, A. Suzuki, H. Murakoshi, N. G. Hedrick, E. Agnello, R. O’Connell, M. M. Stratton, R. Yasuda, Y. Hayashi, (2019) “Reciprocal Activation within a Kinase-Effector Complex Underlying Persistence of Structural LTP” Neuron, 102, 6, P1199-1210.E6. [CellPress]

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, eLife3:e01610. [PubMed]

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 biology23, 292-301. [PubMed]

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, Cell146, 732-745. [PubMed]

M. M. Stratton*, S. McClendon*, D. Eliezer, and S. N. Loh, (2011), Structural characterization of two alternate conformations in a Calbindin D9k-based molecular switch, Biochemistry50, 5583-5589[PubMed]

M. M. Stratton and S. N. Loh, (2011) Converting a protein into a switch for biosensing and functional regulation, Protein Science20, 19-29. [PubMed]

M. M. Stratton and S.N. Loh, (2010) On the mechanism of protein fold-switching by a molecular sensor,Proteins,78, 3260-3269.

M. M. Stratton, T. A. Cutler, J. H. Ha, and S. N. Loh, (2010), Probing local structural fluctuations in myoglobin by size-dependent thiol-disulfide exchange, Protein Science, 19,1587-1594[PubMed]

M. M. Stratton, D. M. Mitrea and S. N. Loh, (2008) A Ca2+-sensing molecular switch based on alternate frame protein folding, ACS Chem. Biol.3, 723-732. [PubMed]