Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA

Author:

Woerner Andreas C.1,Frottin Frédéric1,Hornburg Daniel2,Feng Li R.1,Meissner Felix2,Patra Maria3,Tatzelt Jörg34,Mann Matthias25,Winklhofer Konstanze F.356,Hartl F. Ulrich15,Hipp Mark S.15

Affiliation:

1. Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.

2. Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.

3. Neurobiochemistry, Adolf Butenandt Institute, Ludwig Maximilians University, Schillerstr. 44, D-80336 Munich, Germany.

4. Department of Biochemistry of Neurodegenerative Diseases, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, Universitätsstraße 150, D-44801 Bochum, Germany.

5. Munich Cluster for Systems Neurology (SyNergy), D-80336 Munich, Germany.

6. Department of Molecular Cell Biology, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, Universitätsstraße 150, D-44801 Bochum, Germany.

Abstract

Location, location, location Aggregates of certain disease-associated proteins are involved in neurodegeneration. Woerner et al. now show that the exact location of these aggregates in the cell may be the key to their pathology (see the Perspective by Da Cruz and Cleveland). An artificial aggregate-prone protein caused problems when expressed in the cytoplasm but not when expressed in the nucleus. Cytoplasmic aggregates interfered with nucleocytoplasmic import and export. Perhaps if we can shunt pathological aggregates to the nucleus in the future, we will be able to ameliorate some forms of degenerative disease. Science , this issue p. 173 ; see also p. 125

Funder

European Commission

Munich Cluster for Systems Neurology

German Research Foundation

Hans and Ilse Breuer Foundation

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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