Lan HuangAssistant Professor, Developmental & Cell Biology Assistant Professor, Physiology & Biophysics |
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Research Interests |
biological mass spectrometry/proteomics, ubiquitin-proteasome degradation pathways, protein complexes, posttranslational modifications, protein-protein interaction | |
| URL | Huang lab web page | |
| Appointments |
1996-1997 postdoctoral fellow, Mass Spectrometry Facility, Department of Pharmaceutical Chemistry, University of California, San Francisco 1997-2003 Research specialist, Department of Pharmaceutical Chemistry, Mass Spectrometry Facility, University of California, San Francisco |
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Research Abstract |
The 26S Proteasome is a macromolecular machine responsible for ubiquitin/ATP dependent protein degradation in both cytosol and nucleus. Of the two distinct sub-complexes, the 20S proteasome complex is responsible for various proteolytic activities while the 19S regulatory complex is believed to render ATP-dependent proteolysis of ubiquitinated substrates. Ubiquitin-proteasome dependent protein degradation plays critical roles in numerous essential cellular processes, including cell cycle progression, apoptosis, DNA repair, etc. Recognition and degradation of ubiquitinated substrates including cell cycle regulators, tumor suppressors and transcription factors by the 26S proteasome are tightly regulated to maintain normal cell growth. Because of that, disruption of normal proteasomal degradation pathways can lead to a wide range of human disease, including forms of cancer and neurological degeneration. Recently, the proteasome has become an attractive therapeutic target for the treatment of various cancers. To enrich our understanding of ubiquitin-proteasome degradation pathway for future cancer treatment, we are interested in developing and employing mass spectrometry-based proteomic approaches to identify and characterize the dynamics of both yeast and human 26S proteasome complexes in various biological and pathological processes. The proteomic information obtained in this research will help us understand the mechanisms of ubiquitin-proteasome degradation pathway. In addition, it may provide molecular linkages between various biological processes that are regulated by the ubiquitin-proteasome dependent degradation. Furthermore, the methods developed for the proteasome complex can be applied to the studies of other macromolecular protein complexes. | |
| Publications |
Selected Publications: 1. Guerrero, C., Tagwerker, C., Kaiser, P., Huang, L. An Integrated Mass Spectrometry-Based Proteomics Approach-QTAX to Decipher the 26S Proteasome Interacting Networks. Mol Cell Proteomics. 2006; 5(2):366-78. 2. Tagwerker, C., Flick, K., Cui, M., Gurrero, C., Auer, B., Huang, L., and Kaiser, P. A tandem-affinity tag for two-step purification under fully denaturing conditions. Mol Cell Proteomics., 2006,: 5(4):737-48. 3. Tagwerker, C., Zhang, H., Wang, X., Larsen, L.S., Lathrop, R.H., Hatfield, G.W., Auer, B., Huang, L., Kaiser, P. HB tag modules for PCR-based gene tagging and tandem affinity purification in Saccharomyces cerevisiae. Yeast. 2006;23(8):623-32. 4. Kaiser P, Huang L. Global approaches to understanding ubiquitination. Genome Biol. 2005;6(10):233. 5. Huang, L. and Burlingame, A.L. Comprehensive Mass Spectrometric Analysis of 20S Proteasome Complex. Methods Enzymol. 2005;405:187-236. 6. Chou, S., Huang, L. and Liu, H. Fus3-Regulated Tec1 Degradation through SCF(Cdc4) Determines MAPK Signaling Specificity during Mating in Yeast. Cell. 2004, 119(7):981-90. |
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| Graduate Programs |
Cancer Biology Biomedical Engineering Cell Biology Cellular and Molecular Biosciences |
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| Link to this profile | http://www.faculty.uci.edu/profile.cfm?faculty_id=5268 | |
| Last updated | 09/11/2006 | |