Publications

Selected Publications
Chen S*, Wu J*, Lu Y*, Ma YB, Lee BH, Yu Z, Quyang Q, Finley D, Kirschner M, and Mao Y. (2016) Structural basis for dynamic regulation of the human 26S proteasome. PNAS, 113(46), 12991-12996.

 

Lee BH*, Lu Y, Prado MA, Shi Y, Sun S, Elsasser S, Gygi SP, King RW*, and Finley D*. (2016) USP14 deubiquitinates proteasome-bound substrates that are ubiquitinated at multiple sites. Nature, Apr 21, 532(7599):398-401, doi: 10.1038/nature17433. (* Co-corresponding authors).

 

Shi Y*, Elsasser S*, Stocks BB*, Chen X*, Tian G, Lee BH, Shi Y, Zhang N, de Poot SA, G, Tuebing F, Sun S, Vannoy J, Tarasov SG, Engen JR, Walters KJ, and Finley D. (2016) Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome. Science, Feb 19;351(6275). pii: aad9421. doi: 10.1126/science.aad9421.

 

Xu D, Shan B*, Lee BH*, Zhu K, Zhang T, Sun H, Liu M, Shi L, Liang W, Qian L, Xiao J, Pan L, Finley D, and Yuan J. (2015) Phosphorylation and activation of ubiquitin-specific protease-14 by Akt regulates UPS. eLife, Nov 2;4. pii: e10510. doi: 10.7554/eLife.10510, (* Co-second authors).

 

Lu Y, Lee BH, King RW, Finley D, and Kirschner M (2015) Substrate degradation by the proteasome: a single-molecule kinetic analysis. Science, 348(6231):1250834. doi: 0.1126/science.1250834.

 

Liu YP, Tsai IC, Morleo M, Oh EC, Leitch CC, Massa F, Lee BH, Parker DS, Finley D, Zaghloul NA, Franco B, Katsanis N. (2014) Ciliopathy proteins regulate paracrine signaling by modulating proteasomal degradation of mediators. J. Clin. Invest. 124(5), 2059-2070.

 

Lee BH, Finley D, and King RW. (2012) A High-Throughput Screening Method for Identification of Inhibitors of the Deubiquitinating Enzyme USP14. Curr. Protoc. Chem. Biol. 4, 311-330, John Wiley & Sons, Inc.

 

Dimova N, Hathaway NA, Lee BH, Kirkpatrick DS, Berkowitz ML, Gygi SP, Finley D, and King RW. (2012) APC/C-mediated multiple monoubiquitylation provides an alternative degradation pathway for cyclin B1. Nat. Cell Biol. 14, 168-176.

 

Lee BH*, Lee MJ*, Park S, Oh DC, Elsasser S, Chen PC, Gartner C, Dimova N, Hanna J, Gygi SP, Wilson SM, King RW, and Finley D. (2010) Enhancement of proteasome activity by a small-molecule inhibitor of USP14. Nature 467, 179-184; article; DOI: 10.1038/nature09299. (* Co-first authors).

 

Lee MJ, Lee BH, Hanna J, King RW, and Finley D. (2011) Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes. Mol. Cell. Proteomics 10(5):R110.003871 Epub 2010 Sep 7.

 

Chen X, Lee BH, Finley D, and Walters KJ. (2010) Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2. Mol. Cell 38, 404-415.

 

Roelofs J, Park S, Haas W, Tian G, McAllister FE, Huo Y, Lee BH, Zhang F, Shi Y, Gygi SP, and Finley D. (2009) Chaperone-mediated pathway of proteasome regulatory particle assembly. Nature 459, 861-865.

 

Kim D, Frank CL, Dobbin MM, Tsunemoto RK, Tu W, Peng PL, Guan JS, Lee BH, Moy LY, Giusti P, Broodie N, Mazitschek R, Delalle I, Haggarty SJ, Neve RL, Lu Y, and Tsai LH. (2008) Deregulation of HDAC1 by p25/Cdk5 in neurotoxicity. Neuron 60, 803-817.

 

Lee BH, Chen W, Stippec S, and Cobb MH. (2007) Biological cross-talk between WNK1 and the transforming growth factor -Smad signaling pathway. J. Biol. Chem. 282, 17985-17996.

 

Xu BE, Stippec S, Chu PY, Lazrak A, Li XJ, Lee BH, English JM, Ortega B, Huang CL, and Cobb MH. (2005) WNK1 activates SGK1 to regulate the epithelial sodium channel. Proc. Natl. Acad. Sci. USA 102, 10315-10320.

 

Lenertz L, Lee BH, Min X, Xu BE, Wedin K, Earnest S, Goldsmith EJ, and Cobb MH. (2005) Properties of WNK1 and implications for other family members. J. Biol. Chem. 280, 26653-26658.

 

Xu BE, Lee BH, Min X, Lenertz L, Heise CJ, Stippec S, Goldsmith EJ, and Cobb MH. (2005) WNK1: analysis of protein kinase structure, downstream targets, and potential roles in hypertension. Cell Res. 15, 6-10.

 

Lee BH, Min X, Heise CJ, Xu BE, Chen S, Shu H, Luby-Phelps K, Goldsmith EJ, and Cobb MH. (2004) WNK1 phosphorylates synaptotagmin 2 and modulates its membrane binding. Mol. Cell 15, 741-751.