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Dr. Steve Reichow
Dr. Steve Reichow

Assistant Professor of Chemistry

Ph.D. | University of Washington, 2006

Postdoctoral Fellow | University of Washington, 2007-2011

Postdoctoral Fellow | Howard Hughes Medical Institute, 2011-2014

503-725-7766

reichow@pdx.edu

Research Lab Homepage

 


Research Interests

Research in the Reichow Lab is inspired by the molecular mechanisms driving biology. Our research applies biochemical methods, coupled with high-resolution imaging and structure determination by electron cryo-microscopy (cryoEM) to describe the functional mechanisms of membrane proteins and cell-signaling complexes. We aim to understand membrane protein function, and what goes wrong in disease, by characterizing their mechanisms of action and modes of regulation at the molecular and atomic levels using cryoEM.

Membrane Channel Gating & Cell-Signaling Complexes

We are using cryoEM to describe the functional mechanisms of membrane proteins and cell-signaling complexes. Membrane proteins act as the gatekeepers for the cell, controlling the flow of chemical information across the barrier of a cell membrane. This class of proteins facilitate many complex biological phenomena – from producing the rhythm of our heart beat and transmitting the electro-chemical signals that form our thoughts, to detecting light, sound, touch, as well as our tastes and smells that provide our senses to the world around us. Because of their important biological functions, membrane proteins are among the most heavily targeted class of proteins for fighting disease.

In order to coordinate these complex phenomena, membrane proteins associate with a variety of cell-signaling complexes capable of temporally and spatially regulating their activity. We are keenly interested in understanding the physical mechanisms of how the flow of chemical information that passes through membrane channels gets dynamically modulated (or gated) by various cellular signals (such as calcium, cAMP, and pH) and regulatory proteins (such as calmodulin and various kinases and phosphatase). By providing a mechanistic understanding to the processes regulating membrane proteins, we will enable pharmaceutical and genetic approaches aimed at treating the many pathologies associated with their misregulation.

To learn more – please visit our website (pdx.edu/reichowlab).

Representative Publications

  • Myers JB†, Zaegle V†, Coultrap SJ, Miller A, Bayer KU*, Reichow SL*, The CaMKII holoenzyme structure in activation-competent conformations. Nat Communs. 2017 Jun 7;8:15742

  • Reichow SL, Clemens D, Freites A, Németh-Cahalan KL, Matthias H, Tobias DJ, Hall JE, Gonen T (2013). Calmodulin modulates the water channel gate of aquaporin-0. Nat Struct Mol Biol 20(9):1085-1092. 

  • Smith FD, Reichow SL, Esseltine JL, Shi D, Langeberg LK, Scott JD, Gonen T (2013). Intrinsic disorder within an AKAP-Protein kinase A complex guides local substrate phosphorylation. eLife 2:e01319. 

  • Gold M, Reichow SL, O’Neill SE, Weisbrod CR, Langeberg LK, Bruce JE, Gonen T, Scott JD (2012). AKAP2 anchors PKA with aquaporin-0 to support ocular lens transparency. EMBO Mol Med 4(1):15-26. 

  • Wisedchaisri G, Reichow SL, Gonen T (2011). Advancements in electron crystallography for the study of membrane protein structure and function. Structure 19(10):1381-1393.

  • Reichow SL, Kortokov KV, Gonen M, Sun J, Delarosa JR, Hol WG, Gonen T (2011). The binding of the cholera toxin to the periplasmic vestibule of the type II secretion channel. Channels 5(3):215-218. 

  • Reichow SL, Korotkov KV, Hol WG, Gonen T (2010). Structure of the cholera toxin secretion channel in its closed state. Nat Struct Mol Biol 17(10):1226-32.

  • Reichow SL, Gonen T (2009). Lipid-protein interactions probed by electron crystallography. Curr Opin Struct Biol 19(5):560-5. 

  • Reichow SL, Gonen T (2008). Non-canonical binding of calmodulin to aquaporin-0: implications for channel regulation. Structure 16(9):1389-98. 

  • Andrews S, Reichow SL, Gonen T (2008). Electron crystallography of aquaporins. IUBMB Life 60(7):430-6.