Lamin-binding Proteins
Katherine L. Wilson1 and Roland Foisner2
-Author Affiliations
1Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205
2Max F. Perutz Laboratories, Department of Medical Biochemistry, Medical University of Vienna, Vienna 1030
Correspondence:roland.foisner@meduniwien.ac.at
Abstract
A- and B-type lamins are the major intermediate filaments of the nucleus. Lamins engage in a plethora of stable and transient interactions, near the inner nuclear membrane and throughout the nucleus. Lamin-binding proteins serve an amazingly diverse range of functions. Numerous inner-membrane proteins help anchor lamin filaments to the nuclear envelope, serving as part of the nuclear “lamina” network that is essential for nuclear architecture and integrity. Certain lamin-binding proteins of the inner membrane bind partners in the outer membrane and mechanically link lamins to the cytoskeleton. Inside the nucleus, lamin-binding proteins appear to serve as the “adaptors” by which the lamina organizes chromatin, influences gene expression and epigenetic regulation, and modulates signaling pathways. Transient interactions of lamins with key components of the transcription and replication machinery may provide an additional level of regulation or support to these essential events.
Copyright © 2010 Cold Spring Harbor Laboratory Press; all rights reserved
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