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University of Chicago Postdoctoral Positions at Keenan Lab

 Postdoctoral researchers

We have openings for outstanding scientists who are excited about our research and have a strong background in biochemistry, structural (cryo-EM, x-ray), molecular or cell biology.

Please email Bob for more information.

Department of Biochemistry & Molecular Biology

Gordon Center for Integrative Science Room W238

University of Chicago

929 East 57th Street

Chicago, IL  60637

lab:            (773) 834.2675

office:       (773) 834.2292

fax:            (773) 834.5416

email:       bkeenan@uchicago.edu


Department of Biochemistry & Molecular Biology

Molecular Biosciences

Chemistry & Biology Interfaces

Biophysical Sciences

Committee on Cancer Biology

UChicago Advanced Electron Microscopy facility

Keenan Lab Publications

Substrate-driven assembly of a translocon for multipass membrane proteins

Sundaram, A.#, Yamsek, M.#, Zhong, F.#, Hooda, Y., Hegde, R.S. and Keenan, R.J. (2022)  

Nature, in press. (#=equal contribution) (doi: 10.1038/s41586-022-05330-8)

Mechanism of an intramembrane chaperone for multipass membrane proteins

Smalinskaitė, L.#, Kim, M.K.#, Lewis, A.J.O., Keenan, R.J., and Hegde, R.S. (2022)  

Nature, in press. (#=equal contribution) (doi: 10.1038/s41586-022-05336-2)

The mechanisms of integral membrane protein biogenesis

Hegde, R.S. and Keenan, R.J. (2021) Nature Reviews Molecular Cell Biology. (doi: 10.1038/ s41580-021-00413-2)

An ER translocon for multi-pass membrane protein biogenesis

McGilvray PT, Anghel SA, Sundaram A, Zhong F, Trnka MJ, Fuller JR, Hu H, Burlingame AL, Keenan RJ. (2020)

eLife, Aug 21;9:e56889. (doi: 10.7554/eLife.56889)

The architecture of EMC reveals a path for membrane protein insertion

O'Donnell JP, Phillips BP, Yagita Y, Juszkiewicz S, Wagner A, Malinverni D, Keenan RJ, Miller EA, Hegde RS. (2020)

eLife, May 27;9:e57887. (doi: 10.7554/eLife.57887)

A structural perspective on tail-anchored protein biogenesis by the GET pathway

Mateja, A and Keenan, RJ (2018) Current Opinion in Structural Biology, 51:195-202.

(doi: 10.1016/j.sbi.2018.07.009)

Identification of Oxa1 homologs operating in the eukaryotic endoplasmic reticulum

Anghel, S.A., McGilvray, P.T., Hegde, R.S., Keenan, R.J. (2017) Cell Reports, 21:3708-3716.

(doi:  10.1016/j.celrep.2017.12.006)

Tail-anchored protein insertion by a single Get1/2 heterodimer

Zalisko, B.E., Chan, C., Denic, V., Rock, R.S. and Keenan, R.J. (2017) Cell Reports, 20:2287-2293.

(doi: 10.1016/j.celrep.2017.08.035)

Msp1 is a membrane protein dislocase for tail-anchored proteins

Wohlever ML, Mateja A, McGilvray PT, Day KJ and Keenan, RJ (2017) Molecular Cell, 67:194-202.

(doi: 10.1016/j.molcel.2017.06.019)

The GET system inserts the tail-anchored SYP72 protein into endoplasmic reticulum membranes

Srivistava R, Zalisko BE, Keenan RJ, Howell SH. (2017) Plant Physiol., 173:1137-1145.

(doi: 10.1104/pp.16.00928)

Ubiquilins chaperone and triage mitochondrial membrane proteins for degradation

Itakura, E., Zavodszky, E., Shao, S., Wohlever, M.L., Keenan, R.J., Hegde, R.S. (2016) Molecular Cell, 63:21-33.

(doi: 10.1016/j.molcel.2016.05.020)

Data publication with the structural biology data grid supports live analysis

Meyer PA, Socias S, Key J, Ransey E, Tjon EC, Buschiazzo A, Lei M, Botka C, Withrow J, Neau D, Rajashankar K, Anderson KS, Baxter RH, Blacklow SC, Boggon TJ, Bonvin AM, Borek D, Brett TJ, Caflisch A, Chang CI, Chazin WJ, Corbett KD, Cosgrove MS, Crosson S, Dhe-Paganon S, Di Cera E, Drennan CL, Eck MJ, Eichman BF, Fan QR, Ferré-D'Amaré AR, Fromme JC, Garcia KC, Gaudet R, Gong P, Harrison SC, Heldwein EE, Jia Z, Keenan RJ, Kruse AC, Kvansakul M, McLellan JS, Modis Y, Nam Y, Otwinowski Z, Pai EF, Pereira PJ, Petosa C, Raman CS, Rapoport TA, Roll-Mecak A, Rosen MK, Rudenko G, Schlessinger J, Schwartz TU, Shamoo Y, Sondermann H, Tao YJ, Tolia NH, Tsodikov OV, Westover KD, Wu H, Foster I, Fraser JS, Maia FR, Gonen T, Kirchhausen T, Diederichs K, Crosas M, Sliz P. (2016) Nature Commun., 7:10882. (doi: 10.1038/ncomms10882)

Conformational chaperones for structural studies of membrane proteins using antibody phage display

with nanodiscs

Dominik, P.K., Borowska, M.T., Dalmas, O., Kim, S.S., Perozo, E., Keenan, R.J., Kossiakoff, A.A. (2016) Structure,

24:300-309. (doi: 10.1016/j.str.2015.11.014)

A dual fluorescent reporter for the investigation of methionine mistranslation in live cells

Gomes A.C., Kordala A.J., Strack R., Wang X., Geslain R., Delaney K., Clark W.C., Keenan R.J., Pan T. (2016) RNA,

22:467-476. (doi: 10.1261/rna.054163.115)

A YidC-like protein in the archaeal plasma membrane

Borowska, M.T., Dominik, P.K., Anghel, S.A., Kossiakoff A.A., Keenan R.J. (2015) Structure, 23:1715-1724.

(doi: 10.1016/j.str.2015.06.025)

Structure of the Get3 targeting factor in complex with its membrane protein cargo

Mateja A, Paduch M, Chang H.Y., Szydlowska A, Kossiakoff A.A., Hegde R.S., Keenan R.J. (2015) Science,

347:1152-1155. (doi: 10.1126/science.1261671)

Fission yeast profilin is tailored to facilitate actin assembly by the cytokinesis formin Cdc12

Bestul, A.J., Christensen, J.R., Grzegorzewska, A.P., Burke, T.A., Sees, J.A., Carroll, R.T., Sirotkin, V., Keenan, R.J.,

Kovar, D.R. (2015) Mol Biol Cell. 26:283-93. (doi: 10.1091/mbc.E13-05-0281)

Tail-anchored membrane protein insertion into the endoplasmic reticulum

Hegde, R.S. and Keenan, R.J. (2011) Nature Reviews Molecular Cell Biology, 12:787-798. (doi: 10.1038/nrm3226)

The mechanism of membrane-associated steps in tail-anchored protein insertion

Mariappan, M.#, Mateja, A.#, Dobosz, M., Bove, E., Hegde, R.S., Keenan, R.J. (2011) Nature, 477:61-66.

(doi: 10.1038/nature10362) (#=co-first authors)

A conserved archaeal pathway for tail-anchored membrane protein insertion

Sherrill, J., Mariappan, M., Dominik, P., Hegde, R.S., Keenan, R.J. (2011) Traffic, 12:1119-1123.

(doi: 10.1111/j.1600-0854.2011.01229.x)

Noncytotoxic DsRed derivatives for whole-cell labeling

Strack R.L., Keenan R.J., Glick B.S. (2011) Methods Mol Biol., 699:355-70.

A ribosome-associating factor chaperones tail-anchored membrane proteins

Mariappan M, Li X, Stefanovic S, Sharma A, Mateja A, Keenan R.J., Hegde R.S. (2010) Nature, 466:1120-4.

Chromophore formation in DsRed occurs by a branched pathway

Strack, R.L., Strongin, D.E., Mets, L., Glick, B.S., Keenan, R.J. (2010) J. Am. Chem. Soc., 132:8496-8505.

The structural basis of tail-anchored membrane protein recognition by Get3

Mateja, A., Szlachcic, A., Downing, M.E., Dobosz, M., Mariappan, M., Hegde, R.S., Keenan, R.J. (2009) Nature,

461:361-366. (doi:10.1038/nature08319)

A rapidly maturing far-red derivative of DsRed-Express2 for whole-cell labeling

Strack, R.L., Hein, B., Bhattacharyya, D., Hell, S.W., Keenan, R.J., Glick, B.S. (2009) Biochemistry, 48:8279-8281.

Noncytotoxic orange and red/green derivatives of DsRed-Express2 for whole-cell labeling

Strack, R.L., Bhattacharyya, D., Glick, B.S., Keenan, R.J. (2009) BMC Biotech., 9:32.

A noncytotoxic DsRed variant for whole-cell labeling

Strack, R.L., Strongin, D.E., Bhattacharyya, D., Tao, W., Berman, A., Broxmeyer, H.E., Keenan, R.J., Glick, B.S. (2008)

Nature Methods, 5:955-957.

Spectral diversity of fluorescent proteins from the anthozoan Corynactis californica

Schnitzler, C.E., Keenan, R.J., Matysik, A., Christianson, L.M., McCord, R., Haddock, S.H.D. (2008) Marine Biotech.,


Structural rearrangements near the chromophore influence the maturation speed and brightness of

DsRed variants

Strongin, D.E., Bevis, B., Khuong, N., Downing, M.E., Strack, R.L., Sundaram, K., Glick, B.S., Keenan, R.J. (2007)

Protein Eng. Des. Sel., 20:525-534.

The molecular basis of glyphosate resistance by an optimized microbial acetyltransferase

Siehl, D.L., Castle, L.A., Gorton, R., Keenan, R.J. (2007) J. Biol. Chem., 282:11446-11455.  

DNA Shuffling as a tool for protein crystallization

Keenan, R.J., Siehl, D.L., Gorton, R., Castle, L.A. (2005) Proc. Natl. Acad. Sci. USA, 102:8887-8892.

Evolution of a microbial acetyltransferase for modification of glyphosate:  a novel tolerance strategy

Siehl, D.L., Castle, L.A., Gorton, R., Chen, Y.H., Bertain, S., Cho, H.J., Keenan, R.J., Liu, D., Lassner, M.W. (2005)

Pest Manag. Sci., 61:235-40.

Laboratory-Directed Protein Evolution

Yuan, L., Kurek, I., English, J., Keenan, R.J. (2005) Microbiol. Mol. Biol. Rev., 69:373-392.

Nontransgenic crops from transgenic plants

Keenan, R.J., Stemmer, W.P. (2002)  Nature Biotech., 20:215-216.

The Signal Recognition Particle

Keenan, R.J., Freymann, D.M., Stroud, R.M., Walter, P. (2001) Annu. Rev. Biochem., 70:755-775.

Perspectives:  structural biology.  SRP – where the RNA and membrane worlds meet

Walter, P., Keenan, R.J., Schmitz, U. (2000) Science, 287:1212-1213.

Structure of the phylogenetically most conserved domain of SRP RNA

Schmitz, U., Behrens, S., Freymann, D.M., Keenan, R.J., Lukavsky, P., Walter, P., James, T.L. (1999) RNA,


Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+-GDP

Freymann, D.M., Keenan, R.J., Stroud, R.M., Walter, P. (1999) Nature Struct. Biol., 6:793-801.

Crystal Structure of the Signal Sequence Binding Subunit of the Signal Recognition Particle

Keenan, R.J., Freymann, D.M., Walter, P., Stroud, R.M. (1998) Cell, 94:181-191.

Structure of the conserved GTPase domain of the signal recognition particle

Freymann, D.M., Keenan, R.J., Stroud, R.M., Walter, P. (1997) Nature, 385:361-364.

NMR studies of the most conserved RNA domain of the mammalian signal recognition particle (SRP)

Schmitz, U., Freymann, D.M., James, T.L., Keenan, R.J., Vinayak, R., Walter, P. (1996) RNA, 2:1213-1227.

Structure of a non-peptide inhibitor complexed with HIV-1 PR. Developing a cycle of structure-based drug


Rutenber, E., Fauman, E.B., Keenan, R.J., Fong, S., Furth, P.S., Ortiz de Montellano, P.R., Meng, E., Kuntz, I.D.,

DeCamp, D.L., Salto, R., Rosé, J.R., Craik, C.S., Stroud, R.M. (1993) J. Biol. Chem., 286:15343-15346.

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