Lukasz Joachimiak, Ph.D.

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 utilizes 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.

Undergraduate

Uni of Wisconsin-Madison (2001), Biochemistry

Graduate School

University of Washington (2007), Biochemistry

• Chaperone structual biology
• Molecular recognition and specificity
• Protein (mis)folding in neurodegenerative diseases

Featured Publications

DNAJB8 oligomerization is mediated by an aromatic-rich motif that is dispensable for substrate activity.

Ryder BD, Ustyantseva E, Boyer DR, Mendoza-Oliva A, Kuska MI, Wydorski PM, Macierzynska P, Morgan N, Sawaya MR, Diamond MI, Kampinga HH, Joachimiak LA, Structure 2024 Mar

Network of hotspot interactions cluster tau amyloid folds.

Mullapudi V, Vaquer-Alicea J, Bommareddy V, Vega AR, Ryder BD, White CL, Diamond MI, Joachimiak LA, Nat Commun 2023 Feb 14 1 895

DnaJC7 binds natively folded structural elements in tau to inhibit amyloid formation.

Hou Z, Wydorski PM, Perez VA, Mendoza-Oliva A, Ryder BD, Mirbaha H, Kashmer O, Joachimiak LA, Nat Commun 2021 09 12 1 5338

Regulatory inter-domain interactions influence Hsp70 recruitment to the DnaJB8 chaperone.

Ryder BD, Matlahov I, Bali S, Vaquer-Alicea J, van der Wel PCA, Joachimiak LA, Nat Commun 2021 02 12 1 946

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

Multivalent coiled-coil interactions enable full-scale centrosome assembly and strength.

Rios MU, Bagnucka MA, Ryder BD, Ferreira Gomes B, Familiari NE, Yaguchi K, Amato M, Stachera WE, Joachimiak LA, Woodruff JB, J Cell Biol 2024 Apr 223 4

Hairpin trimer transition state of amyloid fibril.

Sari L, Bali S, Joachimiak LA, Lin MM, Nat Commun 2024 Mar 15 1 2756

J-domain proteins: From molecular mechanisms to diseases.

Marszalek J, De Los Rios P, Cyr D, Mayer MP, Adupa V, Andréasson C, Blatch GL, Braun JEA, Brodsky JL, Bukau B, Chapple JP, Conz C, Dementin S, Genevaux P, Genest O, Goloubinoff P, Gestwicki J, Hammond CM, Hines JK, Ishikawa K, Joachimiak LA, Kirstein J, Liberek K, Mokranjac D, Nillegoda N, Ramos CHI, Rebeaud M, Ron D, Rospert S, Sahi C, Shalgi R, Tomiczek B, Ushioda R, Ustyantseva E, Ye Y, Zylicz M, Kampinga HH, Cell Stress Chaperones 2023 Dec 29 1 21-33

Saturation mutagenesis of α-synuclein reveals monomer fold that modulates aggregation.

Chlebowicz J, Russ W, Chen D, Vega A, Vernino S, White CL, Rizo J, Joachimiak LA, Diamond MI, Sci Adv 2023 Oct 9 43 eadh3457

Anti-tau antibodies targeting a conformation-dependent epitope selectively bind seeds.

Hitt BD, Gupta A, Singh R, Yang T, Beaver JD, Shang P, White CL, Joachimiak LA, Diamond MI, J Biol Chem 2023 Sep 105252

• Endowed Scholar Award
  (2016-2020)