Rexach, Michael - University of California, Santa Cruz - Molecular, Cell & Developmental Biology Faculty

个人简介

B.S., Syracuse University Ph.D., University of California, Berkeley Postdoctorate, Rockefeller University, 1993-1997

研究领域

The Nuclear Pore Complex Our work centers on elucidating the structure and function of the nuclear pore complex (NPC). This is the supramolecular porin structure in the nuclear envelope of all eukaryotes that creates the aqueous channel connecting the cytoplasm and nucleoplasm of the cell. Its main function is to serve as a size-selective gate in the vital flow of macromolecules between these compartments. It is composed of proteins termed nucleoporins, and approximately 450 of them are needed to form each NPC. We have discovered that a defined subset of nucleoporins are natively unfolded (intrinsically disordered), yet can interact with each other to form a quaternary structure held together by weak hydrophobic attractions. Indeed, this network of FG domains functions in vivo as the physical element of the size-selective diffusion barrier in the NPC. We are currently characterizing the dynamic behavior of these natively unfolded nucleoporins and their structural arrangement within the NPC transport conduit using combination of NMR spectroscopy and molecular modeling, guided by an extensive evolutionary analysis of the nucleoporin family in four Saccharomyces strains.

近期论文

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Quantifying nucleoporin stoichiometry inside single nuclear pore complexes in vivo. Mi L, Goryaynov A, Lindquist A, Rexach M, Yang W. Sci Rep. 2015 Mar 23;5:9372. doi: 10.1038/srep09372. Nuclear pore complex protein sequences determine overall copolymer brush structure and function. Ando D, Zandi R, Kim YW, Colvin M, Rexach M, Gopinathan A. Biophys J. 2014 May 6;106(9):1997-2007. doi: 10.1016/j.bpj.2014.03.021. Physical motif clustering within intrinsically disordered nucleoporin sequences reveals universal functional features. Ando D, Colvin M, Rexach M, Gopinathan A. PLoS One. 2013 Sep 16;8(9):e73831. doi: 10.1371/journal.pone.0073831. eCollection 2013. Single-molecule analysis of the recognition forces underlying nucleo-cytoplasmic transport. Rangl M, Ebner A, Yamada J, Rankl C, Tampé R, Gruber HJ, Rexach M, Hinterdorfer P. Angew Chem Int Ed Engl. 2013 Sep 23;52(39):10356-9. doi: 10.1002/anie.201305359. Epub 2013 Sep 5. No abstract available. Prion formation by a yeast GLFG nucleoporin. Halfmann R, Wright JR, Alberti S, Lindquist S, Rexach M. Prion. 2012 Sep-Oct;6(4):391-9. doi: 10.4161/pri.20199. Epub 2012 May 7. [Complex aortic atheroma plaques: study of 71 patients with lacunar infarcts]. Arboix A, Rexach M, Subirà M, Pujadas R. Med Clin (Barc). 2012 Feb 25;138(4):160-4. doi: 10.1016/j.medcli.2011.10.013. Epub 2011 Dec 26. Spanish. A bimodal distribution of two distinct categories of intrinsically disordered structures with separate functions in FG nucleoporins. Yamada J, Phillips JL, Patel S, Goldfien G, Calestagne-Morelli A, Huang H, Reza R, Acheson J, Krishnan VV, Newsam S, Gopinathan A, Lau EY, Colvin ME, Uversky VN, Rexach MF. Mol Cell Proteomics. 2010 Oct;9(10):2205-24. doi: 10.1074/mcp.M000035-MCP201. Epub 2010 Apr 5. Piecing together nuclear pore complex assembly during interphase. Rexach M. J Cell Biol. 2009 May 4;185(3):377-9. doi: 10.1083/jcb.200904022.