Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 7-Day Trial for You or Your Team.

Learn More →

Proteins that bind A-type lamins: integrating isolated clues

Proteins that bind A-type lamins: integrating isolated clues Commentary 979 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: [email protected]) Journal of Cell Science 117, 979-987 Published by The Company of Biologists 2004 doi:10.1242/jcs.01102 Summary What do such diverse molecules as DNA, actin, lamins, and sketch portraits of ternary complexes and retinoblastoma protein and protein kinase Ca all have in functional pathways that might depend on lamins in vivo. common? They and additional partners bind ‘A-type’ On the basis of our limited current knowledge, we propose lamins, which form stable filaments in animal cell nuclei. lamin-associated complexes with multiple components Mutations in A-type lamins cause a bewildering range of relevant to nuclear structure (e.g. emerin, nesprin 1a , tissue-specific diseases, termed ‘laminopathies’, including actin) or signaling and gene regulation (e.g. LAP2a , Emery-Dreifuss muscular dystrophy and the devastating retinoblastoma, E2F-DP heterodimers, genes) as ‘food for Hutchinson-Gilford progeria syndrome, which mimics thought’. Testing these ideas will deepen our understanding premature aging. Considered individually and collectively, of nuclear function and human disease. partners for A-type lamins form four loose http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Cell Science Unpaywall

Proteins that bind A-type lamins: integrating isolated clues

Zastrow, Michael S.; Vlcek, Sylvia; Wilson, Katherine L.
Journal of Cell Science – Mar 1, 2004
Download PDF
9 pages

Loading next page...
 
/lp/unpaywall/proteins-that-bind-a-type-lamins-integrating-isolated-clues-gT42VftgT3

References

References for this paper are not available at this time. We will be adding them shortly, thank you for your patience.

Publisher
Unpaywall
ISSN
0021-9533
DOI
10.1242/jcs.01102
Publisher site
See Article on Publisher Site

Abstract

Commentary 979 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: [email protected]) Journal of Cell Science 117, 979-987 Published by The Company of Biologists 2004 doi:10.1242/jcs.01102 Summary What do such diverse molecules as DNA, actin, lamins, and sketch portraits of ternary complexes and retinoblastoma protein and protein kinase Ca all have in functional pathways that might depend on lamins in vivo. common? They and additional partners bind ‘A-type’ On the basis of our limited current knowledge, we propose lamins, which form stable filaments in animal cell nuclei. lamin-associated complexes with multiple components Mutations in A-type lamins cause a bewildering range of relevant to nuclear structure (e.g. emerin, nesprin 1a , tissue-specific diseases, termed ‘laminopathies’, including actin) or signaling and gene regulation (e.g. LAP2a , Emery-Dreifuss muscular dystrophy and the devastating retinoblastoma, E2F-DP heterodimers, genes) as ‘food for Hutchinson-Gilford progeria syndrome, which mimics thought’. Testing these ideas will deepen our understanding premature aging. Considered individually and collectively, of nuclear function and human disease. partners for A-type lamins form four loose

Journal

Journal of Cell Science – Unpaywall

Published: Mar 1, 2004

There are no references for this article.