UNIVERSITY OF WISCONSIN-MADISON
UW Home | Graduate School Home | MCP Home

MOLECULAR AND CELLULAR PHARMACOLOGY GRADUATE TRAINING PROGRAM Search: 
Photo of Kurt Amann.

Faculty: Kurt Amann, PhD

Dept: Associate Professor, Zoology
Contact: 335 Bock Labs
608-265-3150
kjamann@wisc.edu
Training Areas:
  • Molecular and Cellular Pharmacology
  • Cellular & Molecular Biology Program
 

Research Interests

Image related to research.

Research in the Amann lab focuses on developing a molecular understanding of the mechanisms underlying cell structure and motility. We continue to study machinery that drives forward the leading edge of eukaryotic cells as they crawl across substrates.

We are particularly interested in understanding the numerous functions of a protein called the Arp2/3 complex, which produces new actin filaments that branch from the sites of older filaments in a manner that supports the physical stresses of motility.

The other major focus of the Amann lab is the newly discovered actin homologues in prokaryotes. Bacteria, we now know, use proteins very similar to actin to control their shape, division, and segregtion of genetic material. Because these proteins were so recently discovered, we know almost nothing about how they carry out their roles in cells or what machinery regulates them.

Elucidating the answers to these important questions will be the focus of much of our efforts over the next several years.

Selected publications

(Find further publications on PubMed)

  • Bean GJ, Flickinger ST, Westler WM, McCully ME, Sept D, Weibel DB, Amann KJ. (2009). A22 disrupts the bacterial actin cytoskeleton by directly binding and inducing a low-affinity state in MreB.Biochemistry. 2009 Jun 9;48:4852-7. PMID: 19382805 [PubMed - indexed for MEDLINE]
  • Mayer JA, Amann KJ. (2009). Assembly properties of the Bacillus subtilis actin, MreB. Cell Motil Cytoskeleton. 66(2):109-118. PMID: 19117023 [PubMed - indexed for MEDLINE]
  • Bean GJ, Flickinger ST, Westler WM, McCully ME, Sept D, Weibel DB, and Amann KJ (2009). A22 disrupts the bacterial actin cytoskeleton by directly binding and inducing a low-affinity state in MreB. Biochemistry. 48:4852-4857. PMID: 19382805
  • Mayer JA and Amann KJ (2009). Assembly properties of the Bacillus subtilis actin, MreB. Cell Motil Cytoskeleton 66:109-118. PMID: 19117023
  • Rouiller I, Xu XP, Amann KJ, Egile C, Nickell S, Nicastro D, Li R, Pollard TD, Volkmann N, and Hanein D. (2008). The structural basis of actin filament branching by the Arp2/3 complex. J Cell Biol. 80:887-895. PMID 18316411