Faculty: Kurt Amann, PhD
|Dept:||Associate Professor, Zoology|
|Contact:|| 335 Bock Labs |
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.
- 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
- 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