Faculty
Martin W. Hetzer
Professor
Jesse and Caryl Philips Foundation Chair
Molecular and Cell Biology Laboratory

Molecular and structural organization of the cell nucleus in development, aging and disease
Biogenesis of the nuclear envelope: One of the most dramatic examples of nuclear reorganization can be observed in dividing metazoan cells, in which the nucleus undergoes a cycle of complete disassembly and reformation. The assembly of the nuclear membrane is critical for proper cell cycle progression and establishing the interphase nuclear architecture. Recent studies from our lab have shown that the nuclear envelope (NE) forms by the reshaping of the endoplasmic reticulum (ER), and not as previously believed by vesicle fusion. Using live cell imaging and cell-free reconstitution systems we showed that NE formation is initiated by the binding of ER membranes to chromatin. Intriguingly, DNA-binding membrane proteins of the inner nuclear membrane, which are dispersed into the ER during mitosis, mediate the formation of a closed membrane. Many of these largely uncharacterized proteins have been shown to function in chromatin regulation and directly participate in transcription control, suggesting a mechanistic link between NE formation and post-mitotic chromatin organization.
In addition we provided new insights into the longstanding question of how NPCs are assembled. We established an in vitro assay to study NPC assembly in intact NEs and could show that pores form by a de novo process from both sides of the NE. Most recently we identified an unexpected role of ER shaping proteins in NPC assembly and succeeded in visualizing the biogenesis of single nuclear pores in living cells. The combination of these methods, together with a novel assay that is based on fluorescent nanocrystalls to study biomolecular interactions, allowed us to answer long standing questions of pore biogenesis. Most recently, we found evidence for the existence of two distinct mechanisms of NPC formation in higher eukaryotes. Our results suggest that, in organisms with open mitosis, NPCs assemble by distinct mechanisms to accommodate cell cycle-dependent differences in NE topology.
Age-related defects of nuclear pore complexes (NPCs): Changes in gene activity are part of the cellular aging process, however, the mechanisms that cause age-related alterations in gene expression are poorly understood. We have recently discovered that NPCs, essential multiprotein channels that mediate molecular trafficking between the nucleoplasm and cytoplasm of eukaryotic cells, are extremely long-lived in post-mitotic tissue and deteriorate over time causing a loss of cell compartmentalization in post-mitotic neurons. Our results suggest that nuclear pore deterioration might be a general aging mechanism leading to age-related defects in nuclear function, such as the loss of youthful gene expression programs. Age-dependent deterioration of nuclear pore complex function and the associated failure of the nuclear permeability barrier is characterized by the leaking of cytoplasmic proteins into the nucleoplasm. We detected large filaments inside the 'leaky' nuclei of old mouse and rat neurons, which stained with the cytoplasmic protein tubulin. Strikingly, tubulin-positive intranuclear structures have been linked to various neurological disorders including Parkinson's disease. Thus, nuclear pore deterioration might initiate or contribute to the onset of certain neurodegenerative diseases.
The role of the nuclear pore complex in chromatin organization and gene regulation. Recently we established a new research area in the lab that focuses on the potential role of NPC components in gene regulation. Nuclear chromatin organization plays an important but poorly understood role in the establishment and maintenance of specific gene expression programs in eukaryotic cells. Using Drosophila melanogaster as a model system we discovered an unexpected link between the dynamic organization of NPCs and gene regulation. We have detected several mobile nucleoporins at sites of on-going transcription during development. Strikingly, these chromatin-bound nucleoporins can be found inside the nucleus. Furthermore, the recruitment of nucleoporins to active sites coincides with the onset of transcription and does not depend on the presence of mRNA. Significantly, depletion of these nucleoporins by RNAi resulted in a block of transcription of nucleoporin target genes. In addition, we found a genetic interaction between several nucleoporins and the formation of silent chromatin. Chromatin binding at specific loci, not associated with gene activity, was also observed for several other dynamic nucleoporins. Based on these findings we hypothesize that mobile nucleoporins are key players in gene regulation via their association with chromatin inside the nucleus.
In summary, our results may establish a novel link between nuclear membrane formation and chromatin organization. This could provide new insights into the well-known phenomenon of pathological nuclear architecture and the physiological consequences of aberrant nucleoporin expression observed in various cancer cells. Ultimately, our studies will lead to a better understanding of developmental gene expression and we hope to translate this knowledge into novel strategies to detect nuclei exhibiting aberrant gene activity and to control expression of disease-associated genes.
Education
- Undergraduate degree, University of Vienna, Austria
- PhD, Biochemistry and Genetics, Vienna Biocenter, Austria
- Postdoctoral work at EMBL, Heidelberg, Germany
Awards and Honors
- 2009 ASCINA Award (Austrian Scientists and Scholars in North America)
- Early Career Life Science Award, American Society of Cell Biology 2009
- Ellison Medical Foundation Senior Scholar in Aging (2009-2013)
- American Cancer Society Research Scholar (2009-2013)
- Pew Scholar 2005
- APART fellow 2000-2003
- EMBO long term fellowship 1998-2003
- Austrian science award in Genetics 1997
- Erwin Schroedinger fellowship 1997
Selected Publications
- Savas, J.N., Toyama, B.H., Xu, T., Yates J.R. and Hetzer, M.W. (2012) Extremely long-lived nuclear pore proteins in the rat brain. Science Feb 2 [Epub ahead of print] D'Angelo, M.A., Gomez-Cavazos, J.S., Mei, A., Lackner, D.H. and Hetzer, M.W. (2012) A change in nuclear pore complex composition regulates cell differentiation. Dev Cell 22, 1-13. Talamas, J. and Hetzer, M.W. (2011) POM121 and Sun1 play a role in ealry steps of interphase NPC assembly. J Cell Biol 194: 27-37. Doucet, C., Talamas, J. and Hetzer, M.W. (2010) Cell Cycle Dependent Differences in Nuclear Pore Complex Assembly in Metazoa. Cell 141: 1030-1041. Capelson, M., Liang, Y., Schulte, R., Mair, W, Wagner, U. and Hetzer, M.W. (2010) Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. Cell 140: 372-383. D'Angelo, M.A., Raices, M., Panowski, S.H. and Hetzer, M.W. (2009) Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in post-mitotic cells. Cell 136: 284-295.
Links
Salk News Releases
- Discovery of extremely long-lived proteins may provide insight into cell aging and neurodegenerative diseases, February 3, 2012
- Salk Institute promotes latest generation of extraordinary scientists, April 15, 2011
- Nuclear pores call on different assembly mechanisms at different cell cycle stages, June 10, 2010
- Nuclear pore complexes harbor new class of gene regulators, offer clues to gene expression and cancer, February 4, 2010
- Salk Scientist wins 2009 Aging Research Award from the Ellison Medical Foundation, October 7, 2009
- The breakdown of barriers in old cells may hold clues to aging process, January 22, 2009
- Salk scientists solve mystery behind how nuclear membrane forms during mitosis, September 12, 2007
- Researchers solve mystery of how nuclear pores duplicate before cell division, April 20, 2006

