Krebber, Heike, Prof. Dr.
Professor for Molecular Genetics
- 1996 Dr. rer. nat., Deutsches Krebsforschungszentrum, DKFZ, Heidelberg (Germany)
- 1996 Visiting Scientist, Weizman Institute of Science, Rehovot (Israel)
- 1996-1999 Scientist, Dana-Farber Cancer Institute, Harvard Medical School, Boston (USA)
- 1999-2010 Junior group leader, Institute für Molekularbiologie und Tumorforschung, Philipps-Universität Marburg (Germany)
- 2005 Habilitation in Molecular Biology
- 2006 Heisenberg Fellow
- since 2010 Professor for Molecular Genetics, Georg-August Universität Göttingen (Germany)
Major Research Interests
The compartimentation of eukaryotic cells requires a machinery that is able to transport a great number of molecules into and out of the nucleus in a rapid, accurate and regulated manner. The natural cargos for this machinery are proteins and RNA-protein complexes (RNPs). For the mRNPs it has to be assured that intron containing pre messenger RNAs are retained in the nucleus until processing is completed. Only fully processed and spliced mRNAs are transported into the cytoplasm and translated at the ribosomes. The otherwise resulting gene products can be toxic to cells and harmful to organisms. Several examples exist where not fully processed pre-mRNAs reach the cytoplasm, resulting in diseases like cancer or neurodegenerative diseases. Our projects aim to identify and characterize the requirements for mRNA processing, transport and translation. We want to learn which proteins are associated with the transported RNP, how transport is regulated and how the cell distinguishes between export incompetent and export competent mRNPs. Moreover, we study the principles of mRNA quality control. Saccharomyces cerevisiae has been proven to be a useful model organism for eukaryotic cells and we use a combination of genetics, biochemistry and cell biology to uncover these processes.
Homepage Department/Research Group
Selected Recent Publications
- Zander G, Krebber H (2017) Quick or Quality? How mRNAs escapes nuclear quality control during stress. RNA Biology, Jul 14:1-7. doi: 10.1080/15476286.2017.1345835.
- Zander G, Hackmann A, Bender L, Becker D, Lingner T, Salinas G, Krebber H (2016) mRNA quality control is bypassed for an immediate export of stress responsive transcripts. Nature, 540: 593-596. DOI 10.1038/nature20572.
- Wu H, Becker D, Krebber H (2014) Telomerase RNA TLC1 shuttling to the cytoplasm requires mRNA export factors and is important for telomere maintenance. Cell Rep. 8: 1-9.
- Hackmann A, Wu H, Schneider UM, Meyer K, Jung K, Krebber H (2014) Quality control of spliced mRNAs requires the shuttling SR proteins Gbp2 and Hrb1. Nat Commun. 5:3123.
- Baierlein C, Hackmann A, Gross T, Henker L, Hinz F, Krebber H (2013) Monosome formation during translation initiation requires the serine/arginine-rich protein Npl3. Mol Cell Biol. 33(24):4811-23.
- Hackmann A, Gross T, Baierlein C, Krebber H (2011) The mRNA export factor Npl3 mediates the nuclear export of large ribosomal subunits. EMBO-Rep. doi: 10.1038/embor.2011.155.
- Baierlein C, Krebber H (2010) Translation termination: New factors and insights. RNA-Biology 7:issue 5: 548 – 550.
- Khoshnevis S, Gross T, Rotte C, Baierlein C, Ficner R, Krebber H (2010) The iron-sulfur protein Rli1 functions in translation termination. EMBO-Rep. 11: 214 – 219.
- Gross T, Siepmann A, Sturm D, Windgassen M, Scarelli J, Cole CN, Seedorf M, Krebber H (2007) The DEAD-box RNA-helicase Dbp5 functions in translation termination. Science, 315 (5812): 646-649.
- Windgassen M, Sturm D, Cajigas IJ, González CI, Seedorf M, Bastians H Krebber, H. (2004) Yeast shuttling SR-proteins Npl3p, Gbp2p and Hrb1p are part of the translated mRNAs and Npl3p can function as a translational repressor. Mol. Cell. Biol., 24 (23): 10479-10491.
- Häcker S, Krebber H (2004) Differential export requirements for shuttling SR-type mRNA binding proteins. J. Biol. Chem. 279 (7):5049-5052.
- Windgassen M, Krebber H (2003) Identification of Gbp2p as a novel poly(A)+RNA binding protein in yeast involved in the cytoplasmic delivery of mRNAs. EMBO Rep. 4 (3): 278-283.