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First published online March 2, 2004
doi: 10.1242/10.1242/jcs.01102

Journal of Cell Science 117, 979-987 (2004)
Published by The Company of Biologists 2004
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Commentary

Proteins that bind A-type lamins: integrating isolated clues

Michael S. Zastrow, Sylvia Vlcek and Katherine L. Wilson*

Department of Cell Biology, Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205, USA

* Author for correspondence (e-mail: klwilson{at}jhmi.edu)

What do such diverse molecules as DNA, actin, retinoblastoma protein and protein kinase C{alpha} all have in common? They and additional partners bind `A-type' lamins, which form stable filaments in animal cell nuclei. Mutations in A-type lamins cause a bewildering range of tissue-specific diseases, termed `laminopathies', including Emery-Dreifuss muscular dystrophy and the devastating Hutchinson-Gilford progeria syndrome, which mimics premature aging. Considered individually and collectively, partners for A-type lamins form four loose groups: architectural partners, chromatin partners, gene-regulatory partners and signaling partners. We describe 16 partners in detail, summarize their binding sites in A-type lamins, and sketch portraits of ternary complexes and functional pathways that might depend on lamins in vivo. On the basis of our limited current knowledge, we propose lamin-associated complexes with multiple components relevant to nuclear structure (e.g. emerin, nesprin 1{alpha}, actin) or signaling and gene regulation (e.g. LAP2{alpha}, retinoblastoma, E2F-DP heterodimers, genes) as `food for thought'. Testing these ideas will deepen our understanding of nuclear function and human disease.

Key words: Laminopathy, Emerin, Emery-Dreifuss muscular dystrophy, Hutchinson-Gilford progeria syndrome, Nuclear envelope


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