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Articles

SUN1 Interacts with Nuclear Lamin A and Cytoplasmic Nesprins To Provide a Physical Connection between the Nuclear Lamina and the Cytoskeleton

Farhana Haque, David J. Lloyd, Dawn T. Smallwood, Carolyn L. Dent, Catherine M. Shanahan, Andrew M. Fry, Richard C. Trembath, Sue Shackleton
Farhana Haque
1Department of Genetics
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David J. Lloyd
1Department of Genetics
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Dawn T. Smallwood
1Department of Genetics
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Carolyn L. Dent
1Department of Genetics
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Catherine M. Shanahan
3Department of Medicine, Division of Cardiovascular Medicine, University of Cambridge, Box 110, Addenbrooke's Hospital, Hills Road, Cambridge CB2 2QQ, United Kingdom
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Andrew M. Fry
2Department of Biochemistry, University of Leicester, University Road, Leicester LE1 7RH, United Kingdom
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Richard C. Trembath
1Department of Genetics
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Sue Shackleton
1Department of Genetics
2Department of Biochemistry, University of Leicester, University Road, Leicester LE1 7RH, United Kingdom
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  • For correspondence: ss115@le.ac.uk
DOI: 10.1128/MCB.26.10.3738-3751.2006
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ABSTRACT

Nuclear migration and positioning within cells are critical for many developmental processes and are governed by the cytoskeletal network. Although mechanisms of nuclear-cytoskeletal attachment are unclear, growing evidence links a novel family of nuclear envelope (NE) proteins that share a conserved C-terminal SUN (Sad1/UNC-84 homology) domain. Analysis of Caenorhabditis elegans mutants has implicated UNC-84 in actin-mediated nuclear positioning by regulating NE anchoring of a giant actin-binding protein, ANC-1. Here, we report the identification of SUN1 as a lamin A-binding protein in a yeast two-hybrid screen. We demonstrate that SUN1 is an integral membrane protein located at the inner nuclear membrane. While the N-terminal domain of SUN1 is responsible for detergent-resistant association with the nuclear lamina and lamin A binding, lamin A/C expression is not required for SUN1 NE localization. Furthermore, SUN1 does not interact with type B lamins, suggesting that NE localization is ensured by binding to an additional nuclear component(s), most likely chromatin. Importantly, we find that the luminal C-terminal domain of SUN1 interacts with the mammalian ANC-1 homologs nesprins 1 and 2 via their conserved KASH domain. Our data provide evidence of a physical nuclear-cytoskeletal connection that is likely to be a key mechanism in nuclear-cytoplasmic communication and regulation of nuclear position.

  • Copyright © 2006 American Society for Microbiology
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SUN1 Interacts with Nuclear Lamin A and Cytoplasmic Nesprins To Provide a Physical Connection between the Nuclear Lamina and the Cytoskeleton
Farhana Haque, David J. Lloyd, Dawn T. Smallwood, Carolyn L. Dent, Catherine M. Shanahan, Andrew M. Fry, Richard C. Trembath, Sue Shackleton
Molecular and Cellular Biology Apr 2006, 26 (10) 3738-3751; DOI: 10.1128/MCB.26.10.3738-3751.2006

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SUN1 Interacts with Nuclear Lamin A and Cytoplasmic Nesprins To Provide a Physical Connection between the Nuclear Lamina and the Cytoskeleton
Farhana Haque, David J. Lloyd, Dawn T. Smallwood, Carolyn L. Dent, Catherine M. Shanahan, Andrew M. Fry, Richard C. Trembath, Sue Shackleton
Molecular and Cellular Biology Apr 2006, 26 (10) 3738-3751; DOI: 10.1128/MCB.26.10.3738-3751.2006
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KEYWORDS

Cell Nucleus
Cytoplasm
cytoskeleton
Lamin Type A
Microtubule-Associated Proteins
Nerve Tissue Proteins
Nuclear Proteins

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