Susan Rae Wente, Ph.D.


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Faculty Appointments
Professor of Cell and Developmental Biology University Provost and Vice Chancellor for Academic Affairs
Ph.D., Biochemistry, University of California, Berkeley, CaliforniaB.S., Biochemistry, University of Iowa, Iowa City, Iowa
Office Address
205 Kirkland Hall
Nashville, TN 37240
Research Description
Our goal is to understand the mechanism for highly selective, bidirectional exchange of proteins and RNA between the nucleus and cytoplasm. Nucleocytoplasmic trafficking is essential for cell function, and precisely regulated during cell division, differentiation and death. At the center of the transport mechanism are the nuclear pore complexes (NPCs), large protein machines embedded in the nuclear envelope. We use yeast, cultured human cells, and zebrafish model systems to address three key questions:

(1) What are the molecular determinants for regulated transport through the NPC? By genetic, molecular and biochemical means, we investigate how NPC proteins interact with transport receptors and facilitate movement.
(2) How are nuclear and cytoplasmic events simultaneously coupled to control mRNA fate? During stress and disease responses, gene expression pathways adapt to target specific transcripts for rapid export, translation and turnover. We are investigating potential roles for NPC-associated factors in coordinating this response.
(3) How do disruptions in NPC function directly impact human disease and aging? We have recently identified specific NPC transport mechanisms that are perturbed in disease and aging processes. These discoveries have opened up entirely new and exciting areas of investigation.

This deeper understanding of the NPC machinery and its regulation provides key mechanistic insights to many human health challenges. Through thorough analysis of NPC transport factors, we have directly linked precise steps in mRNA export to motor neuron diseases such as ALS and LCCS1, and we have uncovered specific nuclear transport pathways that influence aging. We predict that further elucidation of the mechanisms for NPC transport and regulation will uncover other pathogenic mechanisms and identify druggable targets for controlling human disease. Overall, our future work will continue to integrate our discoveries from the analysis of single cell machineries into the context of multicellular organism development and pathophysiology.
Research Keywords
Cell biology, nuclear transport, RNA export, organelle assembly, inositol signaling, trafficking, biochemistry, developmental biology, enzyme action, genetics, kinase, knockout, membrane, mutation, neurobiology, protein structure, signal transduction, yeast
Adams RL, Terry LJ, Wente SR. A Novel Saccharomyces cerevisiae FG Nucleoporin Mutant Collection for Use in Nuclear Pore Complex Functional Experiments. G3 (Bethesda). 2016 Jan; 6(1): 51-8. PMID: 26530420, PMCID: PMC4704724, PII: g3.115.023002, DOI: 10.1534/g3.115.023002, ISSN: 2160-1836.

Aditi, Glass L, Dawson TR, Wente SR. An amyotrophic lateral sclerosis-linked mutation in GLE1 alters the cellular pool of human Gle1 functional isoforms. Adv Biol Regul [print-electronic]. 2015 Nov 11/11/2015; PMID: 26776475, PMCID: PMC4864155, PII: S2212-4926(15)30031-2, DOI: 10.1016/j.jbior.2015.11.001, ISSN: 2212-4934.

Casey AK, Chen S, Novick P, Ferro-Novick S, Wente SR. Nuclear pore complex integrity requires Lnp1, a regulator of cortical endoplasmic reticulum. Mol. Biol. Cell [print-electronic]. 2015 Aug 8/1/2015; 26(15): 2833-44. PMID: 26041935, PMCID: PMC4571342, PII: mbc.E15-01-0053, DOI: 10.1091/mbc.E15-01-0053, ISSN: 1939-4586.

Aditi, Folkmann AW, Wente SR. Cytoplasmic hGle1A regulates stress granules by modulation of translation. Mol. Biol. Cell [print-electronic]. 2015 Apr 4/15/2015; 26(8): 1476-90. PMID: 25694449, PMCID: PMC4395128, PII: mbc.E14-11-1523, DOI: 10.1091/mbc.E14-11-1523, ISSN: 1939-4586.

Lord CL, Timney BL, Rout MP, Wente SR. Altering nuclear pore complex function impacts longevity and mitochondrial function in S. cerevisiae. J. Cell Biol. 2015 Mar 3/16/2015; 208(6): 729-44. PMID: 25778920, PMCID: PMC4362458, PII: jcb.201412024, DOI: 10.1083/jcb.201412024, ISSN: 1540-8140.

Kaneb HM, Folkmann AW, Belzil VV, Jao LE, Leblond CS, Girard SL, Daoud H, Noreau A, Rochefort D, Hince P, Szuto A, Levert A, Vidal S, André-Guimont C, Camu W, Bouchard JP, Dupré N, Rouleau GA, Wente SR, Dion PA. Deleterious mutations in the essential mRNA metabolism factor, hGle1, in amyotrophic lateral sclerosis. Hum. Mol. Genet [print-electronic]. 2015 Mar 3/1/2015; 24(5): 1363-73. PMID: 25343993, PMCID: PMC4321443, PII: ddu545, DOI: 10.1093/hmg/ddu545, ISSN: 1460-2083.

Guet D, Burns LT, Maji S, Boulanger J, Hersen P, Wente SR, Salamero J, Dargemont C. Combining Spinach-tagged RNA and gene localization to image gene expression in live yeast. Nat Commun. 2015; 6: 8882. PMID: 26582123, PMCID: PMC4673486, PII: ncomms9882, DOI: 10.1038/ncomms9882, ISSN: 2041-1723.

Adams RL, Terry LJ, Wente SR. Nucleoporin FG domains facilitate mRNP remodeling at the cytoplasmic face of the nuclear pore complex. Genetics [print-electronic]. 2014 Aug; 197(4): 1213-24. PMID: 24931410, PMCID: PMC4125395, PII: genetics.114.164012, DOI: 10.1534/genetics.114.164012, ISSN: 1943-2631.

Burns LT, Wente SR. Casein kinase II regulation of the Hot1 transcription factor promotes stochastic gene expression. J. Biol. Chem [print-electronic]. 2014 Jun 6/20/2014; 289(25): 17668-79. PMID: 24817120, PMCID: PMC4067201, PII: M114.561217, DOI: 10.1074/jbc.M114.561217, ISSN: 1083-351X.

Burns LT, Wente SR. From hypothesis to mechanism: uncovering nuclear pore complex links to gene expression. Mol. Cell. Biol [print-electronic]. 2014 Jun; 34(12): 2114-20. PMID: 24615017, PMCID: PMC4054283, PII: MCB.01730-13, DOI: 10.1128/MCB.01730-13, ISSN: 1098-5549.

Folkmann AW, Dawson TR, Wente SR. Insights into mRNA export-linked molecular mechanisms of human disease through a Gle1 structure-function analysis. Adv Biol Regul [print-electronic]. 2014 Jan; 54: 74-91. PMID: 24275432, PMCID: PMC3932673, PII: S2212-4926(13)00091-2, DOI: 10.1016/j.jbior.2013.10.002, ISSN: 2212-4934.

Folkmann AW, Collier SE, Zhan X, Aditi, Ohi MD, Wente SR. Gle1 functions during mRNA export in an oligomeric complex that is altered in human disease. Cell [print-electronic]. 2013 Oct 10/24/2013; 155(3): 582-93. PMID: 24243016, PMCID: PMC3855398, PII: S0092-8674(13)01160-4, DOI: 10.1016/j.cell.2013.09.023, ISSN: 1097-4172.

Jao LE, Wente SR, Chen W. Efficient multiplex biallelic zebrafish genome editing using a CRISPR nuclease system. Proc. Natl. Acad. Sci. U.S.A [print-electronic]. 2013 Aug 8/20/2013; 110(34): 13904-9. PMID: 23918387, PMCID: PMC3752207, PII: 1308335110, DOI: 10.1073/pnas.1308335110, ISSN: 1091-6490.

Natalizio BJ, Wente SR. Postage for the messenger: designating routes for nuclear mRNA export. Trends Cell Biol [print-electronic]. 2013 Aug; 23(8): 365-73. PMID: 23583578, PMCID: PMC3729607, PII: S0962-8924(13)00050-0, DOI: 10.1016/j.tcb.2013.03.006, ISSN: 1879-3088.

Adams RL, Wente SR. Uncovering nuclear pore complexity with innovation. Cell. 2013 Mar 3/14/2013; 152(6): 1218-21. PMID: 23498931, PMCID: PMC3672239, PII: S0092-8674(13)00276-6, DOI: 10.1016/j.cell.2013.02.042, ISSN: 1097-4172.

Casey AK, Wente SR. Nuclear transport: shifting gears in fungal nuclear and cytoplasmic organization. Curr. Biol. 2012 Oct 10/9/2012; 22(19): R846-8. PMID: 23058806, PII: S0960-9822(12)01008-1, DOI: 10.1016/j.cub.2012.08.043, ISSN: 1879-0445.

Casey AK, Dawson TR, Chen J, Friederichs JM, Jaspersen SL, Wente SR. Integrity and function of the Saccharomyces cerevisiae spindle pole body depends on connections between the membrane proteins Ndc1, Rtn1, and Yop1. Genetics [print-electronic]. 2012 Oct; 192(2): 441-55. PMID: 22798490, PMCID: PMC3454875, PII: genetics.112.141465, DOI: 10.1534/genetics.112.141465, ISSN: 1943-2631.

Burns LT, Wente SR. Nuclear GPS for interchromosomal clustering. Dev. Cell. 2012 Jun 6/12/2012; 22(6): 1119-20. PMID: 22698275, PMCID: PMC3388979, PII: S1534-5807(12)00246-8, DOI: 10.1016/j.devcel.2012.05.019, ISSN: 1878-1551.

Burns LT, Wente SR. Trafficking to uncharted territory of the nuclear envelope. Curr. Opin. Cell Biol [print-electronic]. 2012 Jun; 24(3): 341-9. PMID: 22326668, PMCID: PMC3518394, PII: S0955-0674(12)00010-5, DOI: 10.1016/, ISSN: 1879-0410.

Jao LE, Appel B, Wente SR. A zebrafish model of lethal congenital contracture syndrome 1 reveals Gle1 function in spinal neural precursor survival and motor axon arborization. Development [print-electronic]. 2012 Apr; 139(7): 1316-26. PMID: 22357925, PMCID: PMC3294435, PII: dev.074344, DOI: 10.1242/dev.074344, ISSN: 1477-9129.

Bolger TA, Wente SR. Gle1 is a multifunctional DEAD-box protein regulator that modulates Ded1 in translation initiation. J. Biol. Chem [print-electronic]. 2011 Nov 11/18/2011; 286(46): 39750-9. PMID: 21949122, PMCID: PMC3220593, PII: M111.299321, DOI: 10.1074/jbc.M111.299321, ISSN: 1083-351X.

Folkmann AW, Noble KN, Cole CN, Wente SR. Dbp5, Gle1-IP6 and Nup159: a working model for mRNP export. Nucleus [print-electronic]. 2011 Nov; 2(6): 540-8. PMID: 22064466, PMCID: PMC3324343, PII: 17881, DOI: 10.4161/nucl.2.6.17881, ISSN: 1949-1042.

Wente SR. Spatial and temporal impacts on a career in science. Mol. Biol. Cell. 2011 Nov; 22(21): 3923-5. PMID: 22039063, PMCID: PMC3204050, PII: 22/21/3923, DOI: 10.1091/mbc.E11-05-0446, ISSN: 1939-4586.

Noble KN, Tran EJ, Alcázar-Román AR, Hodge CA, Cole CN, Wente SR. The Dbp5 cycle at the nuclear pore complex during mRNA export II: nucleotide cycling and mRNP remodeling by Dbp5 are controlled by Nup159 and Gle1. Genes Dev. 2011 May 5/15/2011; 25(10): 1065-77. PMID: 21576266, PMCID: PMC3093122, PII: 25/10/1065, DOI: 10.1101/gad.2040611, ISSN: 1549-5477.

Hodge CA, Tran EJ, Noble KN, Alcazar-Roman AR, Ben-Yishay R, Scarcelli JJ, Folkmann AW, Shav-Tal Y, Wente SR, Cole CN. The Dbp5 cycle at the nuclear pore complex during mRNA export I: dbp5 mutants with defects in RNA binding and ATP hydrolysis define key steps for Nup159 and Gle1. Genes Dev. 2011 May 5/15/2011; 25(10): 1052-64. PMID: 21576265, PMCID: PMC3093121, PII: 25/10/1052, DOI: 10.1101/gad.2041611, ISSN: 1549-5477.

Sarmah B, Wente SR. Inositol hexakisphosphate kinase-2 acts as an effector of the vertebrate Hedgehog pathway. Proc. Natl. Acad. Sci. U.S.A [print-electronic]. 2010 Nov 11/16/2010; 107(46): 19921-6. PMID: 20980661, PMCID: PMC2993352, PII: 1007256107, DOI: 10.1073/pnas.1007256107, ISSN: 1091-6490.

Carmody SR, Tran EJ, Apponi LH, Corbett AH, Wente SR. The mitogen-activated protein kinase Slt2 regulates nuclear retention of non-heat shock mRNAs during heat shock-induced stress. Mol. Cell. Biol [print-electronic]. 2010 Nov; 30(21): 5168-79. PMID: 20823268, PMCID: PMC2953050, PII: MCB.00735-10, DOI: 10.1128/MCB.00735-10, ISSN: 1098-5549.

Wente SR, Rout MP. The nuclear pore complex and nuclear transport. Cold Spring Harb Perspect Biol [print-electronic]. 2010 Oct; 2(10): a000562. PMID: 20630994, PMCID: PMC2944363, PII: cshperspect.a000562, DOI: 10.1101/cshperspect.a000562, ISSN: 1943-0264.

Kelly SM, Leung SW, Apponi LH, Bramley AM, Tran EJ, Chekanova JA, Wente SR, Corbett AH. Recognition of polyadenosine RNA by the zinc finger domain of nuclear poly(A) RNA-binding protein 2 (Nab2) is required for correct mRNA 3'-end formation. J. Biol. Chem [print-electronic]. 2010 Aug 8/20/2010; 285(34): 26022-32. PMID: 20554526, PMCID: PMC2924000, PII: M110.141127, DOI: 10.1074/jbc.M110.141127, ISSN: 1083-351X.

Zheng C, Fasken MB, Marshall NJ, Brockmann C, Rubinson ME, Wente SR, Corbett AH, Stewart M. Structural basis for the function of the Saccharomyces cerevisiae Gfd1 protein in mRNA nuclear export. J. Biol. Chem [print-electronic]. 2010 Jul 7/2/2010; 285(27): 20704-15. PMID: 20463024, PMCID: PMC2898303, PII: M110.107276, DOI: 10.1074/jbc.M110.107276, ISSN: 1083-351X.

Noble KN, Wente SR. Nuclear mRNA on the move. Nat. Cell Biol. 2010 Jun; 12(6): 525-7. PMID: 20517300, PII: ncb0610-525, DOI: 10.1038/ncb0610-525, ISSN: 1476-4679.

Alcázar-Román AR, Bolger TA, Wente SR. Control of mRNA export and translation termination by inositol hexakisphosphate requires specific interaction with Gle1. J. Biol. Chem [print-electronic]. 2010 May 5/28/2010; 285(22): 16683-92. PMID: 20371601, PMCID: PMC2878036, PII: M109.082370, DOI: 10.1074/jbc.M109.082370, ISSN: 1083-351X.

Titus LC, Dawson TR, Rexer DJ, Ryan KJ, Wente SR. Members of the RSC chromatin-remodeling complex are required for maintaining proper nuclear envelope structure and pore complex localization. Mol. Biol. Cell [print-electronic]. 2010 Mar 3/15/2010; 21(6): 1072-87. PMID: 20110349, PMCID: PMC2836959, PII: E09-07-0615, DOI: 10.1091/mbc.E09-07-0615, ISSN: 1939-4586.

Sarmah B, Wente SR. Zebrafish inositol polyphosphate kinases: new effectors of cilia and developmental signaling. Adv. Enzyme Regul [print-electronic]. 2010; 50(1): 309-23. PMID: 19914277, PMCID: PMC3753175, PII: S0065-2571(09)00075-2, DOI: 10.1016/j.advenzreg.2009.10.018, ISSN: 1873-2437.

Terry LJ, Wente SR. Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport. Eukaryotic Cell [print-electronic]. 2009 Dec; 8(12): 1814-27. PMID: 19801417, PMCID: PMC2794212, PII: EC.00225-09, DOI: 10.1128/EC.00225-09, ISSN: 1535-9786.

Hetzer MW, Wente SR. Border control at the nucleus: biogenesis and organization of the nuclear membrane and pore complexes. Dev. Cell. 2009 Nov; 17(5): 606-16. PMID: 19922866, PMCID: PMC3746554, PII: S1534-5807(09)00429-8, DOI: 10.1016/j.devcel.2009.10.007, ISSN: 1878-1551.

Beliakova-Bethell N, Terry LJ, Bilanchone V, DaSilva R, Nagashima K, Wente SR, Sandmeyer S. Ty3 nuclear entry is initiated by viruslike particle docking on GLFG nucleoporins. J. Virol [print-electronic]. 2009 Nov; 83(22): 11914-25. PMID: 19759143, PMCID: PMC2772691, PII: JVI.01192-09, DOI: 10.1128/JVI.01192-09, ISSN: 1098-5514.

Carmody SR, Wente SR. MRNA nuclear export at a glance. J. Cell. Sci. 2009 Jun 6/15/2009; 122(Pt 12): 1933-7. PMID: 19494120, PMCID: PMC2723150, PII: 122/12/1933, DOI: 10.1242/jcs.041236, ISSN: 0021-9533.

Dawson TR, Lazarus MD, Hetzer MW, Wente SR. ER membrane-bending proteins are necessary for de novo nuclear pore formation. J. Cell Biol. 2009 Mar 3/9/2009; 184(5): 659-75. PMID: 19273614, PMCID: PMC2686408, PII: jcb.200806174, DOI: 10.1083/jcb.200806174, ISSN: 1540-8140.

Sarmah B, Wente SR. Dual functions for the Schizosaccharomyces pombe inositol kinase Ipk1 in nuclear mRNA export and polarized cell growth. Eukaryotic Cell [print-electronic]. 2009 Feb; 8(2): 134-46. PMID: 19047361, PMCID: PMC2643608, PII: EC.00279-08, DOI: 10.1128/EC.00279-08, ISSN: 1535-9786.

Bolger TA, Folkmann AW, Tran EJ, Wente SR. The mRNA export factor Gle1 and inositol hexakisphosphate regulate distinct stages of translation. Cell. 2008 Aug 8/22/2008; 134(4): 624-33. PMID: 18724935, PMCID: PMC2601711, PII: S0092-8674(08)00779-4, DOI: 10.1016/j.cell.2008.06.027, ISSN: 1097-4172.

Alcázar-Román AR, Wente SR. Inositol polyphosphates: a new frontier for regulating gene expression. Chromosoma [print-electronic]. 2008 Feb; 117(1): 1-13. PMID: 17943301, DOI: 10.1007/s00412-007-0126-4, ISSN: 0009-5915.

Tran EJ, Zhou Y, Corbett AH, Wente SR. The DEAD-box protein Dbp5 controls mRNA export by triggering specific RNA:protein remodeling events. Mol. Cell. 2007 Dec 12/14/2007; 28(5): 850-9. PMID: 18082609, PII: S1097-2765(07)00631-4, DOI: 10.1016/j.molcel.2007.09.019, ISSN: 1097-2765.

Sarmah B, Winfrey VP, Olson GE, Appel B, Wente SR. A role for the inositol kinase Ipk1 in ciliary beating and length maintenance. Proc. Natl. Acad. Sci. U.S.A [print-electronic]. 2007 Dec 12/11/2007; 104(50): 19843-8. PMID: 18056639, PMCID: PMC2148385, PII: 0706934104, DOI: 10.1073/pnas.0706934104, ISSN: 1091-6490.

Terry LJ, Shows EB, Wente SR. Crossing the nuclear envelope: hierarchical regulation of nucleocytoplasmic transport. Science. 2007 Nov 11/30/2007; 318(5855): 1412-6. PMID: 18048681, PII: 318/5855/1412, DOI: 10.1126/science.1142204, ISSN: 1095-9203.

Tran EJ, Bolger TA, Wente SR. SnapShot: nuclear transport. Cell. 2007 Oct 10/19/2007; 131(2): 420. PMID: 17956740, PII: S0092-8674(07)01286-X, DOI: 10.1016/j.cell.2007.10.015, ISSN: 0092-8674.

Terry LJ, Wente SR. Nuclear mRNA export requires specific FG nucleoporins for translocation through the nuclear pore complex. J. Cell Biol [print-electronic]. 2007 Sep 9/24/2007; 178(7): 1121-32. PMID: 17875746, PMCID: PMC2064648, PII: jcb.200704174, DOI: 10.1083/jcb.200704174, ISSN: 0021-9525.

Ryan KJ, Zhou Y, Wente SR. The karyopherin Kap95 regulates nuclear pore complex assembly into intact nuclear envelopes in vivo. Mol. Biol. Cell [print-electronic]. 2007 Mar; 18(3): 886-98. PMID: 17182855, PMCID: PMC1805111, PII: E06-06-0525, DOI: 10.1091/mbc.E06-06-0525, ISSN: 1059-1524.

Hoek KL, Antony P, Lowe J, Shinners N, Sarmah B, Wente SR, Wang D, Gerstein RM, Khan WN. Transitional B cell fate is associated with developmental stage-specific regulation of diacylglycerol and calcium signaling upon B cell receptor engagement. J. Immunol. 2006 Oct 10/15/2006; 177(8): 5405-13. PMID: 17015726, PII: 177/8/5405, ISSN: 0022-1767.

Alcázar-Román AR, Tran EJ, Guo S, Wente SR. Inositol hexakisphosphate and Gle1 activate the DEAD-box protein Dbp5 for nuclear mRNA export. Nat. Cell Biol [print-electronic]. 2006 Jul; 8(7): 711-6. PMID: 16783363, PII: ncb1427, DOI: 10.1038/ncb1427, ISSN: 1465-7392.

Tran EJ, Wente SR. Dynamic nuclear pore complexes: life on the edge. Cell. 2006 Jun 6/16/2006; 125(6): 1041-53. PMID: 16777596, PII: S0092-8674(06)00674-X, DOI: 10.1016/j.cell.2006.05.027, ISSN: 0092-8674.

Miao M, Ryan KJ, Wente SR. The integral membrane protein Pom34p functionally links nucleoporin subcomplexes. Genetics [print-electronic]. 2006 Mar; 172(3): 1441-57. PMID: 16361228, PMCID: PMC1456286, PII: genetics.105.052068, DOI: 10.1534/genetics.105.052068, ISSN: 0016-6731.

Kendirgi F, Rexer DJ, Alcázar-Román AR, Onishko HM, Wente SR. Interaction between the shuttling mRNA export factor Gle1 and the nucleoporin hCG1: a conserved mechanism in the export of Hsp70 mRNA. Mol. Biol. Cell [print-electronic]. 2005 Sep; 16(9): 4304-15. PMID: 16000379, PMCID: PMC1196339, PII: E04-11-0998, DOI: 10.1091/mbc.E04-11-0998, ISSN: 1059-1524.

Sarmah B, Latimer AJ, Appel B, Wente SR. Inositol polyphosphates regulate zebrafish left-right asymmetry. Dev. Cell. 2005 Jul; 9(1): 133-45. PMID: 15992547, PII: S1534-5807(05)00171-1, DOI: 10.1016/j.devcel.2005.05.002, ISSN: 1534-5807.

Miller AL, Suntharalingam M, Johnson SL, Audhya A, Emr SD, Wente SR. Cytoplasmic inositol hexakisphosphate production is sufficient for mediating the Gle1-mRNA export pathway. J. Biol. Chem [print-electronic]. 2004 Dec 12/3/2004; 279(49): 51022-32. PMID: 15459192, PII: M409394200, DOI: 10.1074/jbc.M409394200, ISSN: 0021-9258.

Suntharalingam M, Alcázar-Román AR, Wente SR. Nuclear export of the yeast mRNA-binding protein Nab2 is linked to a direct interaction with Gfd1 and to Gle1 function. J. Biol. Chem [print-electronic]. 2004 Aug 8/20/2004; 279(34): 35384-91. PMID: 15208322, PII: M402044200, DOI: 10.1074/jbc.M402044200, ISSN: 0021-9258.

Kiseleva E, Allen TD, Rutherford S, Bucci M, Wente SR, Goldberg MW. Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments. J. Struct. Biol. 2004 Mar; 145(3): 272-88. PMID: 14960378, PII: S1047847703002879, DOI: 10.1016/j.jsb.2003.11.010, ISSN: 1047-8477.

Strawn LA, Shen T, Shulga N, Goldfarb DS, Wente SR. Minimal nuclear pore complexes define FG repeat domains essential for transport. Nat. Cell Biol [print-electronic]. 2004 Mar; 6(3): 197-206. PMID: 15039779, PII: ncb1097, DOI: 10.1038/ncb1097, ISSN: 1465-7392.

Rayala HJ, Kendirgi F, Barry DM, Majerus PW, Wente SR. The mRNA export factor human Gle1 interacts with the nuclear pore complex protein Nup155. Mol. Cell Proteomics [print-electronic]. 2004 Feb; 3(2): 145-55. PMID: 14645504, PII: M300106-MCP200, DOI: 10.1074/mcp.M300106-MCP200, ISSN: 1535-9476.

Suntharalingam M, Wente SR. Peering through the pore: nuclear pore complex structure, assembly, and function. Dev. Cell. 2003 Jun; 4(6): 775-89. PMID: 12791264, PII: S153458070300162X, ISSN: 1534-5807.

Kendirgi F, Barry DM, Griffis ER, Powers MA, Wente SR. An essential role for hGle1 nucleocytoplasmic shuttling in mRNA export. J. Cell Biol. 2003 Mar 3/31/2003; 160(7): 1029-40. PMID: 12668658, PMCID: PMC2172758, PII: jcb.200211081, DOI: 10.1083/jcb.200211081, ISSN: 0021-9525.

Ryan KJ, McCaffery JM, Wente SR. The Ran GTPase cycle is required for yeast nuclear pore complex assembly. J. Cell Biol [print-electronic]. 2003 Mar 3/31/2003; 160(7): 1041-53. PMID: 12654904, PMCID: PMC2172763, PII: jcb.200209116, DOI: 10.1083/jcb.200209116, ISSN: 0021-9525.

Steger DJ, Haswell ES, Miller AL, Wente SR, O'Shea EK. Regulation of chromatin remodeling by inositol polyphosphates. Science [print-electronic]. 2003 Jan 1/3/2003; 299(5603): 114-6. PMID: 12434012, PMCID: PMC1458531, PII: 1078062, DOI: 10.1126/science.1078062, ISSN: 1095-9203.

Bayliss R, Littlewood T, Strawn LA, Wente SR, Stewart M. GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta. J. Biol. Chem [print-electronic]. 2002 Dec 12/27/2002; 277(52): 50597-606. PMID: 12372823, PII: M209037200, DOI: 10.1074/jbc.M209037200, ISSN: 0021-9258.

Chang SC, Miller AL, Feng Y, Wente SR, Majerus PW. The human homolog of the rat inositol phosphate multikinase is an inositol 1,3,4,6-tetrakisphosphate 5-kinase. J. Biol. Chem [print-electronic]. 2002 Nov 11/15/2002; 277(46): 43836-43. PMID: 12223481, PII: M206134200, DOI: 10.1074/jbc.M206134200, ISSN: 0021-9258.

Ryan KJ, Wente SR. Isolation and characterization of new Saccharomyces cerevisiae mutants perturbed in nuclear pore complex assembly. BMC Genet [print-electronic]. 2002 Sep 9/5/2002; 3: 17. PMID: 12215173, PMCID: PMC126250, ISSN: 1471-2156.

Verbsky, JW, Wilson, MP, Kisseleva, MV, Majerus, PW, Wente, SR. The synthesis of inositol hexakisphosphate: Characterization of human inositol 1,3,4,5,6-pentakisphosphate 2-kinase. J. Biol. Chem. 2002; 277((35)): 31857-62.

Sondermann, H, Ho, AK, Listenberger, LL, Siegers, K, Moarefi, I, Wente, SR, Hartl, FU, Young, JC. Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in S. cerevisiae. J. Biol. Chem. 2002; 277((36)): 33220-7.

Carvalho J, Bertram PG, Wente SR, Zheng XF. Phosphorylation regulates the interaction between Gln3p and the nuclear import factor Srp1p. J. Biol. Chem [print-electronic]. 2001 Jul 7/6/2001; 276(27): 25359-65. PMID: 11331291, PII: M103050200, DOI: 10.1074/jbc.M103050200, ISSN: 0021-9258.

Strawn LA, Shen T, Wente SR. The GLFG regions of Nup116p and Nup100p serve as binding sites for both Kap95p and Mex67p at the nuclear pore complex. J. Biol. Chem [print-electronic]. 2001 Mar 3/2/2001; 276(9): 6445-52. PMID: 11104765, PII: M008311200, DOI: 10.1074/jbc.M008311200, ISSN: 0021-9258.

Feng Y, Wente SR, Majerus PW. Overexpression of the inositol phosphatase SopB in human 293 cells stimulates cellular chloride influx and inhibits nuclear mRNA export. Proc. Natl. Acad. Sci. U.S.A [print-electronic]. 2001 Jan 1/30/2001; 98(3): 875-9. PMID: 11158563, PMCID: PMC14677, PII: 021558098, DOI: 10.1073/pnas.021558098, ISSN: 0027-8424.

Ho AK, Shen TX, Ryan KJ, Kiseleva E, Levy MA, Allen TD, Wente SR. Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p. Mol. Cell. Biol. 2000 Aug; 20(15): 5736-48. PMID: 10891509, PMCID: PMC86051, ISSN: 0270-7306.

Barry DM, Wente SR. Nuclear transport: never-ending cycles of signals and receptors. Essays Biochem. 2000; 36: 89-103. PMID: 12471905, ISSN: 0071-1365.

Ives, EB, Nichols, J, Wente, SR, York, JD. Biochemical and functional characterization of inositol 1,3,4,5, 6-pentakisphosphate 2-kinases. J. Biol. Chem. 2000; 275: 36575-83.

Wente, S. R. Gatekeepers of the nucleus. Science. 2000; 288: 1374-7.

Ryan, K and Wente, SR. The nuclear pore complex: a protein machine bridging the nucleus and cytoplasm. Curr. Opin. Cell Biol. 2000; 12: 361-71.

Odom, A. R., Stahlberg, A., Wente, S. R., York, J. D. A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control. Science. 2000; 287: 2026-9.

York, J. D., Odom, A. R., Murphy, R., Ives, E. B., Wente, S. R. A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export. Science. 1999; 285: 96-100.

Bucci, M., Wente, S. R. A novel fluorescence-based genetic strategy identifies mutants of Saccharomyces cerevisiae defective for nuclear pore complex assembly. Mol. Biol. Cell. 1998; 9: 2439-61.

Watkins, J. L., Murphy, R., Emtage, J. L., Wente, S. R. The human homologue of Saccharomyces cerevisiae Gle1p is required for poly(A)+ RNA export. Proc. Natl. Acad. Sci. USA. 1998; 95: 6779-84.

Ho, A. K., Raczniak, G. A., Ives, E. B., Wente, S. R. The integral membrane protein snl1p is genetically linked to yeast nuclear pore complex function. Mol. Biol. Cell. 1998; 9: 355-73.

Iovine, M. K., Wente, S. R. A nuclear export signal in Kap95p is required for both recycling the import factor and interaction with the nucleoporin GLFG repeat regions of Nup116p and Nup100p. J. Cell Biol. 1997; 137: 797-811.

Emtage, J. L., Bucci, M., Watkins, J. L., Wente, S. R. Defining the essential functional regions of the nucleoporin Nup145p. J. Cell Sci. 1997; 110: 911-25.

Bucci, M., Wente, S. R. In vivo dynamics of nuclear pore complexes in yeast. J. Cell Biol. 1997; 136: 1185-99.

Murphy, R., Watkins, J. L., Wente, S. R. GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces pombe export factor RAE1, is required for nuclear pore complex structure and function. Mol. Biol. Cell. 1996; 7: 1921-37.

Murphy, R., Wente, S. R. An RNA-export mediator with an essential nuclear export signal. Nature. 1996; 383: 357-60.

Iovine, M. K., Watkins, J. L., Wente, S. R. The GLFG repetitive region of the nucleoporin Nup116p interacts with Kap95p, an essential yeast nuclear import factor. J. Cell Biol. 1995; 131: 1699-713.

Rout MP, Wente SR. Pores for thought: nuclear pore complex proteins. Trends Cell Biol. 1994 Oct; 4(10): 357-65. PMID: 14731624, PII: 096289249490085X, ISSN: 0962-8924.

Wente, S. R., Blobel, G. NUP145 encodes a novel yeast glycine-leucine-phenylalanine-glycine (GLFG) nucleoporin required for nuclear envelope structure. J. Cell Biol. 1994; 125: 955-69.

Wente, S. R., Blobel, G. A temperature-sensitive NUP116 null mutant forms a nuclear envelope seal over the yeast nuclear pore complex thereby blocking nucleocytoplasmic traffic. J. Cell Biol. 1993; 123: 275-84.

Wente, S. R., Rout, M. P. , Blobel, G. A new family of yeast nuclear pore complex proteins. J. Cell Biol. 1992; 119: 705-23.

Wente, S. R., Schachman, H. K. Different amino acid substitutions at the same position in the nucleotide-binding site of aspartate transcarbamoylase have diverse effects on the allosteric properties of the enzyme. J. Biol. Chem. 1991; 266: 20833-9.

Wente, S. R., Villalba, R., Schrammm, V. L., Rosen, O. M. Mn2(+)-binding properties of a recombinant protein-tyrosine kinase derived from the human insulin receptor. Proc. Natl. Acad. Sci. USA. 1990; 87: 2805-9.

Wente, S. R., Rosen, O. M. Insulin-receptor approaches to studying protein kinase domain. Diabetes Care. 1990; 13: 280-7.

Villalba, M., Wente, S. R., Russell, D. S., Ahn, J. C., Reichelderfer, C. F., Rosen, O. M. Another version of the human insulin receptor kinase domain: expression, purification, and characterization. Proc. Natl. Acad. Sci. USA. 1989; 86: 7847-52.

Wente, S. R., Schachman, H. K. Shared active sites in oligomeric enzymes: model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis. Proc. Natl. Acad. Sci. USA. 1987; 84: 31-5.

Robey, E. A., Wente, S. R., Markby, D. W., Flint, A., Yang, Y. R., Schachman, H. K. Effect of amino acid substitutions on the catalytic and regulatory properties of aspartate transcarbamoylase. Proc. Natl. Acad. Sci. USA. 1986; 83: 5934-8.

Available Postdoctoral Position Details
Posted: 1/19/2015
My laboratory has funded positions open for excellent scientists at the postdoctoral level who are interested in pursuing the study of nucleocytoplasmic transport. A current curriculum vitae and three letters of reference should be forwarded for consideration.

The scientific projects in my laboratory currently focus on using either yeast S. cerevisiae or mammalian tissue culture, or Xenopus model systems to understand the mechanism of nuclear transport at the molecular level. Toward this goal, the research directives in my laboratory have focused into three subgroups: 1) analyzing the role of nuclear transport factor interactions with the nuclear pore complex, with particular emphasis on either the role of the FG nucleoporins in the general mechanism or the role of the shuttling mRNA export factor Gle1.
2) studying the mechanism of nuclear pore complex assembly and dynamics, with a focus on developing novel fluorescence, genetic, and structural strategies to dissect the pathway of assembly.
3) Understanding how a novel nuclear inositol polyphosphate signaling pathway regulates mRNA export. We speculate that nuclear inositol signaling plays a key role in coordinating mRNA export and gene transcription responses to extracellular stimuli and intracellular cues.