Joe Lutkenhaus, Ph.D.

University Distinguished Professor and Chair
Director of COBRE Program - KUMC
Microbiology, Molecular Genetics and Immunology

Ph.D., University of California-Los Angeles, 1974

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Publications: Click here

lab website

Research Interests

The research in my laboratory is aimed at:

• elucidating the molecular machinery responsible for cell division in bacteria and
• determination of the temporal and spatial regulatory mechanisms necessary to ensure that the septum is placed at midcell and that newborn cells each receive a copy of the chromosome. Our work with the bacterium E. coli has led to the discovery of a cytoskeletel element, the Z ring, that directs septation in all prokaryotic organisms. The Z ring is formed by the self assembly of FtsZ, the ancestral homologue of tubulin.

Our present work involves:

• characterization of FtsZ assembly in vitro;
• mechanisms involved in positioning the Z ring at the division site; and
• determination of assembly pathways for other cell division proteins that are localized to the division site.

Selected Publications

Wu, W., K-T Park, J. Kuecker, T. Holyoak and J. Lutkenhaus. (2011) Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC. Molecular Microbiology 79:1515-28.

Park, K-T, W. Wu, K.P. Battaile, S. Lovell, T. Holyoak and J. Lutkenhaus. (2011) The Min oscillator uses MinD dependent changes in MinE to spatially regulate cytokinesis. Cell 146:396-407. (selected by Faculty of 1000)

Pichoff, S., B. Shen, B. Sullivan and J. Lutkenhaus. (2012) FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins. Molecular Microbiology 83:151-67 (selected by Faculty of 1000)

Park, K-T, W. Wu, S. Lovell and J. Lutkenhaus. (2012) Mechanism of the asymmetric activation of the MinD ATPase by MinE. Molecular Microbiology 85:271-81.

Lutkenhaus, J. MinD and ParA put things in their place. (2012) Trends in Microbiology 20:411-8.

Lutkenhaus, J., S. Pichoff and S. Du. (2012) Bacterial cytokinesis: from Z ring to divisome. Cytoskeleton 69:778-9.

Du, Shishen and J. Lutkenhaus. (2014) SlmA antagonism of FtsZ ring assembly employs a two-pronged mechanism like MinCD. PLOS Genetics 10(7):e1004460.

Du, Shishen, K-T Park and J. Lutkenhaus. (2015) Oligomerization of FtsZ converts the FtsZ tail motif (CCTP) into a multivalent ligand with high avidity for partners ZipA and SlmA. Molecular Microbiology 95:173-88.

Pichoff, S., S. Du and J. Lutkenhaus. (2015) The bypass of ZipA by overexpression of FtsN requires apreviously unknown conserved FtsN motif essential for FtsA-FtsN interaction supporting a model in which FtsA monomers recruit late cell division proteins to the Z ring. Molecular Microbiology 95:971-987.

Park, K-T, S. Du and J. Lutkenhaus. (2015) MinC/MinD copolymers are not required for Min function. Molecular Microbiology 95:173-188.

Du, S., S. Pichoff and J. Lutkenhaus. (2016) FtsEX acts on FtsA to regulate divisome assembly and activity in E. coli. Proc. Natl. Acad. Sci. USA 113(34):E5052-61.
 
Du, S., and J. Lutkenhaus. (2017) The N-succinyl-L, L-diaminopimelic acid desuccinylase DapE acts through ZapB to enhance the Ter signal in Escherichia coli. Molecular Microbiology 105:326-345.
 
Park, K-T, M.T. Villar, A. Artigues and J. Lutkenhaus (2017) MinE conformational dynamics regulate membrane binding, MinD interaction, and Min oscillation. Proc. Natl. Acad. Sci. USA 114:7497-7504.
 
Park, K-T, A. Dajkovic, M. Wissel, Shishen Du and J. Lutkenhaus. (2018) MinC and FtsZ mutant analysis provides insight into MinC/MinD-mediated Z Ring disassembly. J. Biol. Chem. 293:5834-5846.
 
Pichoff, S., S. Du and J. Lutkenhaus. (2018) Disruption of divisome assembly rescued by FtsN-FtsA interaction in Escherichia coli. Proc. Natl. Acad. Sci. USA 115:E6855-E6862.
 
Du, S., S. Pichoff, K. Kruse and J. Lutkenhaus. (2018) FtsZ filaments have the opposite kinetic polarity of microtubules. Proc. Natl. Acad. Sci. USA (in press).