Lehrstuhl für Zell- und Entwicklungsbiologie

Manfred Alsheimer

Manfred Alsheimer

... is a molecular cell biologist with major interest in nuclear structure and dynamics. He graduated from Julius-Maximilians-University of Würzburg where he also received a doctorate in biology. Following a short postdoctoral period and an appropriate time as research project leader in 2006 he habilitated in Cell and Developmental Biology at the Faculty of Biology. Since 2006 Manfred Alsheimer is an independent reserach group leader at the Department of Cell and Developmental Biology at the Julius-Maximilians-University of Würzburg. Finally, in 2013 he was appointed apl. Professor at the University of Würzburg.

2013 appointed apl. Professor

since 2006 Research Group Leader, Dept. Cell and Developmental Biology, University of Würzburg

2006 Habilitation at the Faculty of Biology, University of Würzburg

2000-2006 Assistant Professor, Dept. Cell and Developmental Biology,University of Würzburg

1997-2000 Postdoc, Dept. Cell and Developmental Biology, University of Würzburg

1997 Dr. rer. nat, University of Würzburg

 

manfred.alsheimer(at)uni-wuerzburg.de

Tel +49 (0)931 31-84282

Fax +49 (0)931 31-84252

Room C104

 

Students    Tue, 10:30-11:30 a.m.

Research synopsis

During his graduate studies Manfred Alsheimer already became highly fascinated by cell biology and particularly in nuclear structure and dynamics, a topic which still remaines at the center of his interest. Manfred Alsheimer’s group is mainly working on mammalian germ cells. Germ cells are characterized by a series of quite pronounced dynamic nuclear remodeling processes and thus represent a highly impressing model suitable for studying purposive nuclear reorganization. In particular, segregation of the homologous chromosomes, which marks the central feature of meiotic genome haploidization, essentially depends on an accurate prearrangement of chromosomes that culminates in a precise and unambiguous pairing of the homologs. Pairing with the right partner goes along with, moreover it implicitly requires, vigorous movements of the chromosomes that follow a unique but evolutionarily highly conserved choreography. Remarkably, these movements are driven by the chromosomal ends. Telomeres firmly attach to the nuclear envelope and move to congregate in a small cluster, hence trailing chromosomes into close vicinity, a condition that is suggested to promote homolog recognition and alignment. Thus, the nuclear envelope for its part holds a somehow exceptional but very central role in providing a dynamic platform for meiotic telomere and chromosome movements. A second prominent feature of germ cell development is the characteristic shaping of the sperm nucleus during sperm head formation. It is a well-directed process that requires an elaborate cooperation of different cellular mechanisms and involves assembly of sperm-specific cytoskeletal structures, chromatin compaction, nuclear movement as well as a striking polarization of nuclear components. Recent studies suggest that the nuclear envelope could be a critical and central determinant in sperm head formation. In this context the group of Manfred Alsheimer currently studies the role and impact of particular nuclear envelope components in sperm-specific nuclear shaping and elongation. Since most of these components are expressed not only in germ cells but (at least as related splice forms) in many other cell types these results will also provide important and more general insights into the question how a cell defines nuclear morphology and shape.

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>link to lab page

Selected Publications

Thoma, H., Grünewald, L., Braune, S., Pasch, E., and Alsheimer, M. (2023). SUN4 is a spermatid type II inner nuclear membrane protein that forms heteromeric assemblies with SUN3 and interacts with lamin B3. J. Cell Sci. 136, jcs.260155. doi.org/10.1242/jcs.260155

Pasch, E., Link, J., Beck, C., Scheuerle, S., and Alsheimer, M. (2015). The LINC complex component Sun4 plays a crucial role in sperm head formation and fertility. Biol. Open 4, 1792-1802. doi: 10.1242/bio.015768

Link, J., Leubner, M., Schmitt, J., Göb, E., Benavente, R., Jeang, K.-T., Xu, R., and Alsheimer, M. (2014). Analysis of meiosis in SUN1 deficient mice reveals a distinct role of SUN2 in mammalian meiotic LINC complex formation and function. PLoS Genet. 10, e1004099. doi: 10.1371/journal.pgen.1004099

Link, J., Jahn, D., Schmitt, J., Göb, E., Baar, J., Ortega, S., Benavente, R., and Alsheimer, M. (2013). The meiotic nuclear lamina regulates chromosome dynamics and promotes efficient homologous recombination in the mouse. PLoS Genet. 9, e1003261. doi: 10.1371/journal.pgen.1003261

Kracklauer, M.P., Link, J., and Alsheimer, M. (2013). LINCing the Nuclear Envelope to Gametogenesis. Curr. Top. Dev. Biol. 102, 127-157. doi: 10.1016/B978-0-12-416024-8.00005-2

Fraune, J.1, Alsheimer, M.1*, Volff, J.N., Busch, K., Fraune, S., Bosch, T.C.G., and Benavente, R.* (2012). Hydra meiosis reveals unexpected conservation of structural synaptonemal complex proteins across metazoans. Proc. Natl. Acad. Sci. USA 109, 16588-16593. doi: 10.1073/pnas.1206875109

Jahn, D., Schramm, S., Schnölzer, M., Heilmann, C.J., de Koster, C.G., Schütz, W., Benavente, R., and Alsheimer, M. (2012). A truncated lamin A in the Lmna (-/-) mouse line: Implications for the understanding of laminopathies. Nucleus 3, 463-474. doi: 10.4161/nucl.21676

Göb, E., Schmitt, J., Benavente, R., and Alsheimer, M. (2010). Mammalian sperm head formation involves different polarization of two novel LINC complexes. PLoS ONE 5, e12072. doi: 10.1371/journal.pone.0012072

Schmitt, J., Benavente, R., Hodzic, D., Höög, C., Stewart, C.L., and Alsheimer, M. (2007). Transmembrane protein Sun2 is involved in tethering mammalian meiotic telomeres to the nuclear envelope. Proc. Natl. Acad. Sci. USA 104, 7426-7431. doi: 10.1073/pnas.0609198104

Alsheimer, M., von Glasenapp, E., Hock, R., and Benavente, R. (1999). Architecture of the nuclear periphery of rat pachytene spermatocytes: Distribution of nuclear envelope proteins in relation to synaptonemal complex attachment sites. Mol. Biol. Cell 10, 1235-1245. doi: 10.1091/mbc.10.4.1235 

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