Biography

Download Curriculum Vitae

Lukasz Joachimiak received his B.S. in Biochemistry from the University of Wisconsin-Madison in 2000.  He received his Ph.D. in 2007 working in the lab of David Baker at University of Washington where he established computational tools to define the energetic and structural principles that underlie protein-protein interactions.  He completed his postdoctoral work with Judith Frydman at Stanford University where he developed innovative approaches to understand the structure and mechanics of substrate interaction by the eukaryotic chaperonin TRiC/CCT.

At UT Southwestern Medical Center, Dr. Joachimiak's laboratory will utilize structural and biochemical approaches to dissect the role of chaperones and protein misfolding in neurodegenerative diseases.  His group is also interested in integrating experimental and computational methods to predict the structures of protein complexes not tractable by classical structural biology techniques.

 

 

 

Education

Undergraduate
Uni of Wisconsin-Madison (2001), Biochemistry
Graduate School
University of Washington (2007), Biochemistry

Research Interest

  • Chaperone structual biology
  • Molecular recognition and specificity
  • Neurodegeneration

Publications

Featured Publications LegendFeatured Publications

Tau local structure shields an amyloid-forming motif and controls aggregation propensity.
Chen D, Drombosky KW, Hou Z, Sari L, Kashmer OM, Ryder BD, Perez VA, Woodard DR, Lin MM, Diamond MI, Joachimiak LA, Nat Commun 2019 06 10 1 2493
The Chaperonin TRiC/CCT Associates with Prefoldin through a Conserved Electrostatic Interface Essential for Cellular Proteostasis.
Gestaut D, Roh SH, Ma B, Pintilie G, Joachimiak LA, Leitner A, Walzthoeni T, Aebersold R, Chiu W, Frydman J, Cell 2019 Apr 177 3 751-765.e15
The ATP-powered gymnastics of TRiC/CCT: an asymmetric protein folding machine with a symmetric origin story.
Gestaut D, Limatola A, Joachimiak L, Frydman J, Curr. Opin. Struct. Biol. 2019 Apr 55 50-58
Inert and seed-competent tau monomers suggest structural origins of aggregation.
Mirbaha H, Chen D, Morazova OA, Ruff KM, Sharma AM, Liu X, Goodarzi M, Pappu RV, Colby DW, Mirzaei H, Joachimiak LA, Diamond MI Elife 2018 Jul 7
Structure and Dynamics of the Huntingtin Exon-1 N-Terminus: A Solution NMR Perspective.
Baias M, Smith PE, Shen K, Joachimiak LA, Zerko S, Kozminski W, Frydman J, Frydman L J. Am. Chem. Soc. 2017 Jan 139 3 1168-1176
xTract: software for characterizing conformational changes of protein complexes by quantitative cross-linking mass spectrometry.
Walzthoeni T, Joachimiak LA, Rosenberger G, Röst HL, Malmström L, Leitner A, Frydman J, Aebersold R Nat. Methods 2015 Dec 12 12 1185-90
The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT.
Joachimiak LA, Walzthoeni T, Liu CW, Aebersold R, Frydman J Cell 2014 Nov 159 5 1042-55
Chemical cross-linking/mass spectrometry targeting acidic residues in proteins and protein complexes.
Leitner A, Joachimiak LA, Unverdorben P, Walzthoeni T, Frydman J, Förster F, Aebersold R Proc. Natl. Acad. Sci. U.S.A. 2014 Jul 111 26 9455-60
Exogenous delivery of chaperonin subunit fragment ApiCCT1 modulates mutant Huntingtin cellular phenotypes.
Sontag EM, Joachimiak LA, Tan Z, Tomlinson A, Housman DE, Glabe CG, Potkin SG, Frydman J, Thompson LM Proc. Natl. Acad. Sci. U.S.A. 2013 Feb 110 8 3077-82
A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle.
Reissmann S, Joachimiak LA, Chen B, Meyer AS, Nguyen A, Frydman J Cell Rep 2012 Oct 2 4 866-77

Honors & Awards

  • Endowed Scholar Award
    (2016-2020)