Kurt J. Amann, Ph.D. Assistant Professor Department of Zoology kjamann@wisc.edu

Research Interests: 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: Article on Pubmed

• 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
  
  
• Bean GJ and Amann KJ. (2008). Polymerization properties of the Thermotoga maritima actin MreB: roles of temperature, nucleotides, and ions. Biochem. 47:826-835. PMID 18095710
  
  
• Perrin BJ, Amann KJ, and Huttenlocher A. (2006). Proteolysis of cortactin by calpain regulates membrane protrusion during cell migration. Mol Biol Cell. 17:239-50. PDF PMID 16280362
  
  
• Maul RS, Song Y, Amann KJ, Gerbin SC, Pollard TD, and Chang DD. (2003). EPLIN regulates actin dynamics by crosslinking and stabilizing filaments. J Cell Biol. 160:399-407. PDF PMID 12566430
  
  
• Amann KJ and Pollard TD. (2001). Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy. PNAS. 98:15009-15013. PDF PMID 11742068
  
  
• Volkmann N, Amann KJ, Stoilova-McPhie S, Egile C, Winter DC, Hazelwood L, Heuser JE, Li R, Pollard TD, and Hanein D. (2001). Structure of the Arp2/3 complex and its actin-bound form at branch junctions. Science. 293:2456-2459. PDF PMID 11533442
  
  
• Amann KJ and Pollard TD. (2001). The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments. Nature Cell Biology. 3:306-310. PDF PMID 11231582
  
  
• Amann KJ and Pollard TD. (2000). Cellular Regulation of Actin Network Assembly. Current Biology. 10:R728-730. PDF PMID 11069094
  
  
• Blanchoin L*, Amann KJ*, Higgs HN, Marchand J-B, Kaiser DA, and Pollard TD. (2000). Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins. Nature. 404:1007-1011. *These authors contributed equally to this work. PDF PMID 10801131
  
  
• Amann KJ, Guo A W-X, and Ervasti JM. (1999). Utrophin lacks the rod domain actin binding activity of dystrophin. J Biol Chem. 274:35375-35380. PDF PMID 10585405
  
  
• Renley BA, Rybakova IN, Amann KJ, and Ervasti JM. (1998). Dystrophin binding to nonmuscle actin. Cell Motil Cytoskeleton. 41:264-70. PMID 9829780
  
  
• Amann KJ, Renley BA, and Ervasti JM. (1998). A cluster of basic repeats in the dystrophin rod domain binds F-actin through an electrostatic interaction. J Biol Chem. 273: 28419-28423. PDF PMID 9774469
  
  
• Ervasti JM, Rybakova IN, and Amann KJ. (1997). A multiple site, side binding model for the interaction of dystrophin with F-actin. Soc Gen Physiol Ser. 52:31-44. PMID 9210218
  
  
• Rybokova IN, Amann KJ, and Ervasti JM. (1996). A new model for the interaction of dystrophin with F-actin. J Cell Biol. 135:661-672. PMID 8909541

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