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Rensselaer Polytechnic Institute Department of Biological Sciences
Susan P. Gilbert
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Department of Biological Sciences
1W14 Jonsson-Rowland Science Center
Rensselaer Polytechnic Institute
110 Eighth Street
Troy, NY 12180-3590

Phone: (518) 276-6446
Fax: (518) 276-2344

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Biology Home Undergraduate Graduate Faculty Research News and Events Contacts
Susan P. Gilbert

Professor and Head, Department of Biological Sciences

Education and Training

A.B. Randolph-Macon Woman’s College, Lynchburg, VA

Ph.D. Dartmouth College
Cell Biology

Dr. Gilbert trained as a Postdoctoral Fellow with Dr. Kenneth Johnson at Pennsylvania State University, University Park, PA, and joined the faculty in the Department of Biological Sciences at the University of Pittsburgh in 1995.  Dr. Gilbert moved to Rensselaer in 2007.

Dr. Gilbert is a fellow of American Association for the Advancement of Science and member of the American Society for Cell Biology, the American Society for Biochemistry and Molecular Biology, and the Biophysical Society. She is on the editorial boards for the Biophysical Journal, and the Journal of Biological Chemistry.


Tel: (518) 276-4415

Office: 2237 Center for Biotechnology & Interdisciplinary Studies
Rensselaer Polytechnic Institute
110 8th Street
Troy, NY 12180

Research Interests

Structure and mechanisms of microtubule-based molecular motors involved in cell motility and cytoskeletal dynamics.

Dr. Gilbert’s lab is interested in cellular movements, and the molecular motors that drive these movements. These remarkable nanoscale machines are involved in diverse biological processes ranging from neuronal development and axoplasmic transport to muscle contraction, meiosis, mitosis, cytokinesis, signal transduction as well as transport of membrane, messenger RNA, and proteins. These molecular motors, regardless of their biological function, all have the ability to convert chemical energy into motion. My research is directed at one family of biological motors, the kinesin superfamily, to ask how these enzymes, fueled by ATP turnover, interact with their microtubule track. These kinesins can pull a cellular cargo along a microtubule, slide one microtubule relative to another, or even remodel the microtubule cytoskeleton by shortening or destabilizing the microtubules. In addition, there are kinesins that actually lengthen the microtubules by adding on tubulin subunits to one end of the microtubule. Yet, these kinesin motors are tiny—for example the catalytic engine is only a few nanometers in diameter.

Our experimental tools include rapid mixing instruments (chemical quench-flow and stopped-flow) that can mix reactants on the millisecond time scale to quantify individual chemical reaction steps that occur as kinesin interacts with the microtubule. For a single event, the motor must attach to the microtubule, generate force through a series of structural transitions, and then detach from the microtubule for the next cycle. Coupled to this mechanical cycle is a chemical cycle of ATP binding, ATP hydrolysis, and release of the products, ADP and inorganic phosphate (Pi). Our research has revealed that variation in the coupling mechanism of ATP turnover to subtle differences in structure account for the remarkable specificity and diversity in kinesin-powered mechanical events. The knowledge gained by this research is expected to be important in applications such as drug discovery and development, nanoscale devices, and regenerative medicine.

Current projects focus on several important kinesin motors, including the following: 

  • Kinesin, an ATPase that drives axoplasmic vesicle movement to the synapse.
  • Ncd, a Drosophila meiotic and mitotic spindle motor. 
  • Kar3Cik1, the yeast microtubule depolymerase required for nuclear fusion during mating.
  • Kar3Vik1, a budding yeast kinesin involved in mitotic spindle assembly and function.
  • Eg5, a spindle motor essential for mitotic spindle assembly and function.
  • CENP-E, a spindle motor essential for chromosome congression.

Selected Publications

Sardar, HS, and SP Gilbert (2012).  Microtubule Capture by Mitotic Kinesin Centromere Protein E (CENP-E).  J. Biol. Chem.  287, 24894-24904. 

Rank, KC, CJ Chen, J Cope, K Porche, A Hoenger, SP Gilbert, and I Rayment (2012).  Kar3Vik1, a Member of the Kinesin-14 Superfamily Shows a Novel Kinesin Microtubule Binding Pattern.  J. Cell Biol.  197, 957-970. 

Gilbert, SP, and HS Sardar (2012).  Kinesin Structure and Biochemistry.  In:  Edward H. Egelman, editor: Comprehensive Biophysics, Vol 4, Molecular Motors and Motility, Yale E. Goldman, E. Michael Ostap.  Oxford:  Academic Press, 2012.  pp. 321-344.

Chen, CJ, I Rayment, SP Gilbert (2011). Kinesin Kar3Cik1 ATPase Pathway for Microtubule Cross-linking. J. Biol. Chem. 286, 29261-29272.

Sardar, HS, VG Luczak, MM Lopez, BC Lister, SP Gilbert (2010). Mitotic Kinesin CENP-E Promotes Microtubule Plus-End Elongation. Curr. Biol. 20, 1648-1653.

McIntosh JR, MK Morphew, PM Grissom, SP Gilbert, A Hoenger (2009). Lattice Structure of Cytoplasmic Microtubules in a Cultured Mammalian Cell. J. Mol. Biol. 394, 177-82.

Krzysiak, TC, M Grabe, and SP Gilbert (2008). Getting in sync with dimeric Eg5. Initiation and regulation of the processive run. J. Biol. Chem. 283, 2078-2087.

Krzysiak, TC, and SP Gilbert (2006). Dimeric Eg5 Maintains Processivity Through Alternating-site Catalysis with Rate-limiting ATP Hydrolysis. J. Biol. Chem. 281, 39444-39454.

Krzysiak, TC, T Wendt, LR Sproul, P Tittman, H Gross, SP Gilbert, and A Hoenger (2006). A Structural Model for Monastrol Inhibition of Dimeric Kinesin Eg5. EMBO J. 25, 2263-2273.

Valentine, MT, PM Fordyce, TC Krzysiak, SP Gilbert, and SM Block (2006). Individual Dimers of the Mitotic Kinesin Motor Eg5 Step Processively and Support Substantial Loads in vitro. Nature Cell Biol. 8, 470-476.

Valentine, MT, and SP Gilbert (2007). To Step or Not to Step? How Biochemistry and Mechanics Influence Processivity in Kinesin and Eg5. Curr. Opin. Cell Biol. 19, 75-81.

Allingham, JA, LR Sproul, I. Rayment, and SP Gilbert (2007). Vik1 Modulates Microtubule-Kar3 Interactions Through a Motor Domain That Lacks an Active Site. Cell 128, 1161-1172.

Sproul, LR, DJ Anderson, AT Mackey, WS Saunders, and SP Gilbert (2005). Cik1 Targets the Minus- end Kinesin Depolymerase Kar3 to the Microtubule Plus-ends. Curr. Biol. 15, 1420-1427.

Cui, W, LR Sproul, SM Gustafson, HJG Matthies, SP Gilbert, and RS Hawley (2005). Drosophila Nod Protein Binds Preferentially to the Plus Ends of Microtubules and Promotes Microtubule Polymerization in vitro. Mol Biol Cell 16, 5400-5409.

Klumpp, LM, A Hoenger, and SP Gilbert (2004). Kinesin’s Second Step. PNAS 101, 3444-3449

Rensselaer Polytechnic Institute Department of Biological Sciences