Harold Paul Erickson

James B. Duke Distinguished Professor Emeritus

Recent research has been on cytoskeleton (eukaryotes and bacteria); a skirmish to debunk the irisin story; a reinterpretation of proposed multivalent binders of the coronavirus spike protein. I have also published an ebook on "Principles of Protein-Protein Association" suitable for a course module or individual learning.

Appointments and Affiliations

  • James B. Duke Distinguished Professor Emeritus
  • Professor Emeritus of Cell Biology

Contact Information

Education

  • Ph.D. Johns Hopkins University, 1968

Research Interests

Cytoskeleton: A major research interest has been the cytoskeleton, in particular microtubules in eukaryotes, and the bacterial tubulin homolog FtsZ. Highlights of our research have been reconstituting FtsZ-rings in liposomes and the demonstration that FtsZ alone can generate a constriction force (Ozawa 2008, 2013); a computer model that explains both treadmilling and nucleation of FtsZ protofilaments based on GTP hydrolysis and the R to T conformational change (Corbin 2020); a perspective linking microtubule growth to the single protofilaments of FtsZ (Erickson 2019).

Irisin. We believe the irisin story is bunk. Irisin was proposed in 2012 as a novel myokine, secreted by muscle cells in response to exercise, it induces the transformation of white fat to brown fat. This inspired hopes of an exercise pill that might correct obesity and other metabolic disorders. We have argued that the original discovery was flawed in several respects (Erickson, Adipocyte, 2013), and that the 1,000+ published follow-up studies are based on flawed commercial antibodies (Albrecht et al, Sci Rep 2015). Our recent review (Maak et al, Endoc Rev 2021) expands these critiques, adds new ones, and suggests that gene knockouts will help resolve controversies.

Sars-CoV-2: Several labs have developed antibody mimics that bind the spike protein, and then incorporated these into dimers and trimers that were designed to bind multivalently to the trimeric spike. We found that the linkers connecting the Nbs are too short to span the distance. We suggest an alternative mechanism for the modest (modest) enhanced avidity (Erickson and Corbin, 2022)

Principles of Protein-Protein Association, Erickson 2019: This ebook, published by IOP press and available to many institutions with a subscription, provides basic principles and discussion of seminal papers. It is suitable for a short course, or for individual learning.

Courses Taught

  • CMB 710E: Cell & Molecular Biology Module V

In the News

Representative Publications

  • Lemmon, Christopher A., Tomoo Ohashi, and Harold P. Erickson. “Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility.” J Biol Chem 286, no. 30 (July 29, 2011): 26375–82. https://doi.org/10.1074/jbc.M111.240028.
  • Osawa, Masaki, and Harold P. Erickson. “Inside-out Z rings--constriction with and without GTP hydrolysis.” Mol Microbiol 81, no. 2 (July 2011): 571–79. https://doi.org/10.1111/j.1365-2958.2011.07716.x.
  • Chen, Yaodong, and Harold P. Erickson. “Conformational changes of FtsZ reported by tryptophan mutants.” Biochemistry 50, no. 21 (May 31, 2011): 4675–84. https://doi.org/10.1021/bi200106d.
  • Erickson, Harold P., David E. Anderson, and Masaki Osawa. “FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.” Microbiol Mol Biol Rev 74, no. 4 (December 2010): 504–28. https://doi.org/10.1128/MMBR.00021-10.
  • Erickson, Harold P., and Masaki Osawa. “Cell division without FtsZ--a variety of redundant mechanisms.” Mol Microbiol 78, no. 2 (October 2010): 267–70. https://doi.org/10.1111/j.1365-2958.2010.07321.x.
  • Popp, David, Mitsusada Iwasa, Harold P. Erickson, Akihiro Narita, Yuichiro Maéda, and Robert C. Robinson. “Suprastructures and dynamic properties of Mycobacterium tuberculosis FtsZ.” J Biol Chem 285, no. 15 (April 9, 2010): 11281–89. https://doi.org/10.1074/jbc.M109.084079.
  • Osawa, Masaki, David E. Anderson, and Harold P. Erickson. “Curved FtsZ protofilaments generate bending forces on liposome membranes.” EMBO J 28, no. 22 (November 18, 2009): 3476–84. https://doi.org/10.1038/emboj.2009.277.
  • Kenjale, Roma, Guoyu Meng, Doran L. Fink, Twyla Juehne, Tomoo Ohashi, Harold P. Erickson, Gabriel Waksman, and Joseph W. St Geme. “Structural determinants of autoproteolysis of the Haemophilus influenzae Hap autotransporter.” Infect Immun 77, no. 11 (November 2009): 4704–13. https://doi.org/10.1128/IAI.00598-09.
  • Sontag, Christopher A., Harvey Sage, and Harold P. Erickson. “BtubA-BtubB heterodimer is an essential intermediate in protofilament assembly.” PLoS One 4, no. 9 (September 29, 2009): e7253. https://doi.org/10.1371/journal.pone.0007253.
  • Chen, Yaodong, and Harold P. Erickson. “FtsZ filament dynamics at steady state: subunit exchange with and without nucleotide hydrolysis.” Biochemistry 48, no. 28 (July 21, 2009): 6664–73. https://doi.org/10.1021/bi8022653.
  • Erickson, Harold P. “Modeling the physics of FtsZ assembly and force generation.” Proc Natl Acad Sci U S A 106, no. 23 (June 9, 2009): 9238–43. https://doi.org/10.1073/pnas.0902258106.
  • Ohashi, Tomoo, Anne Marie Augustus, and Harold P. Erickson. “Transient opening of fibronectin type III (FNIII) domains: the interaction of the third FNIII domain of FN with anastellin.” Biochemistry 48, no. 19 (May 19, 2009): 4189–97. https://doi.org/10.1021/bi900001g.
  • Erickson, Harold P. “Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy.” Biol Proced Online 11 (May 15, 2009): 32–51. https://doi.org/10.1007/s12575-009-9008-x.
  • Popp, David, Mitsusada Iwasa, Akihiro Narita, Harold P. Erickson, and Yuichiro Maéda. “FtsZ condensates: an in vitro electron microscopy study.” Biopolymers 91, no. 5 (May 2009): 340–50. https://doi.org/10.1002/bip.21136.
  • Ohashi, Tomoo, and Harold P. Erickson. “Revisiting the mystery of fibronectin multimers: the fibronectin matrix is composed of fibronectin dimers cross-linked by non-covalent bonds.” Matrix Biol 28, no. 3 (April 2009): 170–75. https://doi.org/10.1016/j.matbio.2009.03.002.
  • Osawa, Masaki, and Harold P. Erickson. “Chapter 1 - Tubular liposomes with variable permeability for reconstitution of FtsZ rings.” Methods Enzymol 464 (2009): 3–17. https://doi.org/10.1016/S0076-6879(09)64001-5.
  • Xu, Jielin, Eunnyung Bae, Qinghong Zhang, Douglas S. Annis, Harold P. Erickson, and Deane F. Mosher. “Display of cell surface sites for fibronectin assembly is modulated by cell adherence to (1)F3 and C-terminal modules of fibronectin.” PLoS One 4, no. 1 (2009): e4113. https://doi.org/10.1371/journal.pone.0004113.
  • White, Glenn E., and Harold P. Erickson. “The coiled coils of cohesin are conserved in animals, but not in yeast.” PLoS One 4, no. 3 (2009): e4674. https://doi.org/10.1371/journal.pone.0004674.
  • Takahashi, Seiichiro, Michael Leiss, Markus Moser, Tomoo Ohashi, Tomoe Kitao, Dominik Heckmann, Alexander Pfeifer, et al. “The RGD motif in fibronectin is essential for development but dispensable for fibril assembly.” J Cell Biol 178, no. 1 (July 2, 2007): 167–78. https://doi.org/10.1083/jcb.200703021.
  • Ohashi, Tomoo, Stephane D. Galiacy, Gina Briscoe, and Harold P. Erickson. “An experimental study of GFP-based FRET, with application to intrinsically unstructured proteins.” Protein Sci 16, no. 7 (July 2007): 1429–38. https://doi.org/10.1110/ps.072845607.
  • Erickson, Harold P. “Evolution of the cytoskeleton.” Bioessays 29, no. 7 (July 2007): 668–77. https://doi.org/10.1002/bies.20601.
  • Osawa, Masaki, and Harold P. Erickson. “FtsZ from divergent foreign bacteria can function for cell division in Escherichia coli.” J Bacteriol 188, no. 20 (October 2006): 7132–40. https://doi.org/10.1128/JB.00647-06.
  • White, Glenn E., and Harold P. Erickson. “Sequence divergence of coiled coils--structural rods, myosin filament packing, and the extraordinary conservation of cohesins.” J Struct Biol 154, no. 2 (May 2006): 111–21. https://doi.org/10.1016/j.jsb.2006.01.001.
  • Osawa, Masaki, and Harold P. Erickson. “Probing the domain structure of FtsZ by random truncation and insertion of GFP.” Microbiology (Reading) 151, no. Pt 12 (December 2005): 4033–43. https://doi.org/10.1099/mic.0.28219-0.
  • Ohashi, Tomoo, and Harold P. Erickson. “Domain unfolding plays a role in superfibronectin formation.” J Biol Chem 280, no. 47 (November 25, 2005): 39143–51. https://doi.org/10.1074/jbc.M509082200.
  • Chen, Yaodong, and Harold P. Erickson. “Rapid in vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer.” J Biol Chem 280, no. 23 (June 10, 2005): 22549–54. https://doi.org/10.1074/jbc.M500895200.
  • Sontag, Christopher A., James T. Staley, and Harold P. Erickson. “In vitro assembly and GTP hydrolysis by bacterial tubulins BtubA and BtubB.” J Cell Biol 169, no. 2 (April 25, 2005): 233–38. https://doi.org/10.1083/jcb.200410027.
  • Redick, Sambra D., Jesse Stricker, Gina Briscoe, and Harold P. Erickson. “Mutants of FtsZ targeting the protofilament interface: effects on cell division and GTPase activity.” J Bacteriol 187, no. 8 (April 2005): 2727–36. https://doi.org/10.1128/JB.187.8.2727-2736.2005.
  • Chen, Yaodong, Keith Bjornson, Sambra D. Redick, and Harold P. Erickson. “A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus.” Biophys J 88, no. 1 (January 2005): 505–14. https://doi.org/10.1529/biophysj.104.044149.
  • Anderson, David E., Frederico J. Gueiros-Filho, and Harold P. Erickson. “Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins.” J Bacteriol 186, no. 17 (September 2004): 5775–81. https://doi.org/10.1128/JB.186.17.5775-5781.2004.
  • Ohashi, Tomoo, and Harold P. Erickson. “The disulfide bonding pattern in ficolin multimers.” J Biol Chem 279, no. 8 (February 20, 2004): 6534–39. https://doi.org/10.1074/jbc.M310555200.
  • Stricker, Jesse, and Harold P. Erickson. “In vivo characterization of Escherichia coli ftsZ mutants: effects on Z-ring structure and function.” J Bacteriol 185, no. 16 (August 2003): 4796–4805. https://doi.org/10.1128/JB.185.16.4796-4805.2003.
  • Ohashi, Tomoo, Daniel P. Kiehart, and Harold P. Erickson. “Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants.” J Cell Sci 115, no. Pt 6 (March 15, 2002): 1221–29. https://doi.org/10.1242/jcs.115.6.1221.
  • Stricker, Jesse, Paul Maddox, E. D. Salmon, and Harold P. Erickson. “Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching.” Proc Natl Acad Sci U S A 99, no. 5 (March 5, 2002): 3171–75. https://doi.org/10.1073/pnas.052595099.
  • Erickson, Harold P. “Stretching fibronectin.” J Muscle Res Cell Motil 23, no. 5–6 (2002): 575–80. https://doi.org/10.1023/a:1023427026818.
  • Erickson, H. P. “Gamma-tubulin nucleation: template or protofilament?” Nat Cell Biol 2, no. 6 (June 2000): E93–96. https://doi.org/10.1038/35014084.
  • Redick, S. D., D. L. Settles, G. Briscoe, and H. P. Erickson. “Defining fibronectin's cell adhesion synergy site by site-directed mutagenesis.” J Cell Biol 149, no. 2 (April 17, 2000): 521–27. https://doi.org/10.1083/jcb.149.2.521.
  • Ohashi, T., D. P. Kiehart, and H. P. Erickson. “Dynamics and elasticity of the fibronectin matrix in living cell culture visualized by fibronectin-green fluorescent protein.” Proc Natl Acad Sci U S A 96, no. 5 (March 2, 1999): 2153–58. https://doi.org/10.1073/pnas.96.5.2153.
  • Ohashi, T., and H. P. Erickson. “Oligomeric structure and tissue distribution of ficolins from mouse, pig and human.” Arch Biochem Biophys 360, no. 2 (December 15, 1998): 223–32. https://doi.org/10.1006/abbi.1998.0957.
  • Melby, T. E., C. N. Ciampaglio, G. Briscoe, and H. P. Erickson. “The symmetrical structure of structural maintenance of chromosomes (SMC) and MukB proteins: long, antiparallel coiled coils, folded at a flexible hinge.” J Cell Biol 142, no. 6 (September 21, 1998): 1595–1604. https://doi.org/10.1083/jcb.142.6.1595.
  • O’Brien, E. T., E. D. Salmon, and H. P. Erickson. “How calcium causes microtubule depolymerization.” Cell Motil Cytoskeleton 36, no. 2 (1997): 125–35. https://doi.org/10.1002/(SICI)1097-0169(1997)36:23.0.CO;2-8.
  • Leahy, D. J., I. Aukhil, and H. P. Erickson. “2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region.” Cell 84, no. 1 (January 12, 1996): 155–64. https://doi.org/10.1016/s0092-8674(00)81002-8.
  • Erickson, H. P., D. W. Taylor, K. A. Taylor, and D. Bramhill. “Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers.” Proc Natl Acad Sci U S A 93, no. 1 (January 9, 1996): 519–23. https://doi.org/10.1073/pnas.93.1.519.
  • Erickson, H. P. “Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin.” Proc Natl Acad Sci U S A 91, no. 21 (October 11, 1994): 10114–18. https://doi.org/10.1073/pnas.91.21.10114.
  • Erickson, H. P. “Gene knockouts of c-src, transforming growth factor beta 1, and tenascin suggest superfluous, nonfunctional expression of proteins.” J Cell Biol 120, no. 5 (March 1993): 1079–81. https://doi.org/10.1083/jcb.120.5.1079.
  • Leahy, D. J., W. A. Hendrickson, I. Aukhil, and H. P. Erickson. “Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein.” Science 258, no. 5084 (November 6, 1992): 987–91. https://doi.org/10.1126/science.1279805.
  • Northrup, S. H., and H. P. Erickson. “Kinetics of protein-protein association explained by Brownian dynamics computer simulation.” Proc Natl Acad Sci U S A 89, no. 8 (April 15, 1992): 3338–42. https://doi.org/10.1073/pnas.89.8.3338.
  • Erickson, H. P. “Co-operativity in protein-protein association. The structure and stability of the actin filament.” J Mol Biol 206, no. 3 (April 5, 1989): 465–74. https://doi.org/10.1016/0022-2836(89)90494-4.
  • Walker, R. A., E. T. O’Brien, N. K. Pryer, M. F. Soboeiro, W. A. Voter, H. P. Erickson, and E. D. Salmon. “Dynamic instability of individual microtubules analyzed by video light microscopy: rate constants and transition frequencies.” J Cell Biol 107, no. 4 (October 1988): 1437–48. https://doi.org/10.1083/jcb.107.4.1437.
  • Erickson, H. P., and J. L. Inglesias. “A six-armed oligomer isolated from cell surface fibronectin preparations.” Nature 311, no. 5983 (September 20, 1984): 267–69. https://doi.org/10.1038/311267a0.
  • Voter, W. A., and H. P. Erickson. “The kinetics of microtubule assembly. Evidence for a two-stage nucleation mechanism.” J Biol Chem 259, no. 16 (August 25, 1984): 10430–38.
  • Fowler, W. E., and H. P. Erickson. “Trinodular structure of fibrinogen. Confirmation by both shadowing and negative stain electron microscopy.” J Mol Biol 134, no. 2 (October 25, 1979): 241–49. https://doi.org/10.1016/0022-2836(79)90034-2.
  • Erickson, H. P. “Microtubule surface lattice and subunit structure and observations on reassembly.” J Cell Biol 60, no. 1 (January 1974): 153–67. https://doi.org/10.1083/jcb.60.1.153.