Huang, Lan - University of California, Irvine - Department of Biological Chemistry

个人简介

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 2003-2009 Assistant Professor, Depts. of Physiology & Biophysics and Developmental & Cell Biology 2009-2012 Associate Professor, Depts. of Physiology & Biophysics and Developmental & Cell Biology 7/2012- Professor, Dept of Physiology & Biophysics

研究领域

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.

近期论文

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Kao, A.#, Randall, A.#, Patel, V., Yang, Y., Kandur, W., Guan, S., Rychnovsky, S., Baldi, P., Huang, L. Mapping the structural topology of the yeast 19S proteasomal regulatory particle using chemical cross-linking and probabilistic modeling. Mol. Cell. Proteomics 2012, Apr 30. [Epub ahead of print] (#: These authors contributed equally) Fang, L.#, Kaake, R#., Patel, V., Yang, Y., Baldi, P., Huang, L. Mapping the protein interaction network of the human COP9 signalosome (CSN) complex using a label-free QTAX strategy. Mol. Cell. Proteomics 2012, 11(5), 138-47. (#: These authors contributed equally). Xu, J., Reddy, B.J., Anand, P., Shu, Z., Cermelli, S., Mattson, M.K., Tripathy, S.K., Hoss, M.T., James, N.S., King, S.J., Huang, L., Bardwell, L., Gross, S.P. Casein kinase 2 reverses tail-independent inactivation of kinesin-1. Nat. Commun. 2012, 3, 754. doi: 10.1038/ncomms1760. Guo, X., Engela, J.L., Xiaoa, J., Tagliabraccib, V.S., Wang, X., Huang, L., Dixon, J. E. UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity. Proc. Natl. Acad. Sci. U S A 2011, 108(46), 18649-54. (It was reported in UCSD news, http://ucsdnews.ucsd.edu/newsrel/health/2011_09dixon.asp) Wu, K., Yan, H., Fang, L., Wang, X., Pfleger, C., Jiang, X., Huang, L., Pan, Z.Q. Mono-ubiquitination drives nuclear export of the human Dcn1-like protein hDCNL1. J Biol Chem. 2011, 286(39), 34060-70