Cellular and Molecular Life Sciences CMLS

, Volume 60, Issue 8, pp 1607–1612

Intermediate filaments: novel assembly models and exciting new functions for nuclear lamins

Visions & Reflections

DOI: 10.1007/s00018-003-3004-0

Cite this article as:
Herrmann, H. & Foisner, R. CMLS, Cell. Mol. Life Sci. (2003) 60: 1607. doi:10.1007/s00018-003-3004-0

Abstract

Intermediate filament (IF) proteins constitute a highly diverse family of fibrous proteins in metazoans, which assemble into 10-nm-thick filaments in the cytoplasm and the nucleus. Novel recent insights into the in vitro assembly mechanism have revealed principal differences in the formation of cytoplasmic and nuclear filaments. Moreover, the past years have seen dramatic developments for the nuclear specific IF proteins, the lamins. While in the past lamins have been assumed to form only a structural scaffold at the nuclear periphery, their discovery in the nuclear interior, the identification of novel lamin-binding proteins and the functional disruption of lamin structures have brought to light essential functions for lamins in fundamental cellular events such as chromatin organization, DNA replication and RNA transcription. Furthermore, mutations in lamins and lamin-binding proteins have been demonstrated to cause various different human diseases, affecting muscle, heart, neuronal, adipose and bone tissue or leading to premature ageing. However, the molecular basis of these diseases is just beginning to emerge.

Chromatincoiled coilsfilament assemblylaminalamina-associated proteinslaminopathynuclear membraneunit-lenght filaments

Copyright information

© Birkhäuser-Verlag Basel 2003

Authors and Affiliations

  1. 1.German Cancer Research Center (DKFZ)Division of Cell Biology, Technology Park 3, 1.308Heidelberg
  2. 2.ViennaBiocenter, University of ViennaDepartment of Medical Biochemistry, Section of Molecular Cell BiologyVienna