Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 30 November 2007:
Vol. 318. no. 5855, pp. 1408 - 1412
DOI: 10.1126/science.1142034
Prev | Table of Contents | Next

Review

Blurring the Boundary: The Nuclear Envelope Extends Its Reach

Colin L. Stewart,1 Kyle J. Roux,2 Brian Burke2*

The past decade has seen a complete rethinking of the traditional view of the nuclear envelope as simply a passive enclosure for the chromosomes. The convergence of several lines of clinical and basic research has revealed additional roles in both signaling and mitotic progression. It is becoming apparent that the nuclear envelope defines not only nuclear organization but also that of the cytoskeleton and, in this way, integrates both nuclear and cytoplasmic architecture.

1 Institute of Medical Biology, 61 Biopolis Drive, Proteos, Singapore 138668, Singapore.
2 Department of Anatomy and Cell Biology, The University of Florida, 1600 Southwest Archer Road, Gainesville, FL 32610–0235, USA.

* To whom correspondence should be addressed. E-mail. bburke{at}ufl.edu

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
A perinuclear actin cap regulates nuclear shape.
S. B. Khatau, C. M. Hale, P. J. Stewart-Hutchinson, M. S. Patel, C. L. Stewart, P. C. Searson, D. Hodzic, and D. Wirtz (2009)
PNAS 106, 19017-19022
   Abstract »    Full Text »    PDF »
Overlapping Functions of Nuclear Envelope Proteins NET25 (Lem2) and Emerin in Regulation of Extracellular Signal-Regulated Kinase Signaling in Myoblast Differentiation.
M. D. Huber, T. Guan, and L. Gerace (2009)
Mol. Cell. Biol. 29, 5718-5728
   Abstract »    Full Text »    PDF »
NET37, a Nuclear Envelope Transmembrane Protein with Glycosidase Homology, Is Involved in Myoblast Differentiation.
K. Datta, T. Guan, and L. Gerace (2009)
J. Biol. Chem. 284, 29666-29676
   Abstract »    Full Text »    PDF »
Bringing KASH under the SUN: the many faces of nucleo-cytoskeletal connections.
D. Razafsky and D. Hodzic (2009)
J. Cell Biol. 186, 461-472
   Abstract »    Full Text »    PDF »
KDP-1 is a nuclear envelope KASH protein required for cell-cycle progression.
M. D. McGee, I. Stagljar, and D. A. Starr (2009)
J. Cell Sci. 122, 2895-2905
   Abstract »    Full Text »    PDF »
Nuclear Fusion and Genome Encounter during Yeast Zygote Formation.
A. M. Tartakoff and P. Jaiswal (2009)
Mol. Biol. Cell 20, 2932-2942
   Abstract »    Full Text »    PDF »
Mechanisms of RNA-mediated Disease.
J. R. O'Rourke and M. S. Swanson (2009)
J. Biol. Chem. 284, 7419-7423
   Abstract »    Full Text »    PDF »
Requirement for Sun1 in the expression of meiotic reproductive genes and piRNA.
Y.-H. Chi, L. I. Cheng, T. Myers, J. M. Ward, E. Williams, Q. Su, L. Faucette, J.-Y. Wang, and K.-T. Jeang (2009)
Development 136, 965-973
   Abstract »    Full Text »    PDF »
A nuclear-envelope bridge positions nuclei and moves chromosomes.
D. A. Starr (2009)
J. Cell Sci. 122, 577-586
   Abstract »    Full Text »    PDF »
Nesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization.
K. J. Roux, M. L. Crisp, Q. Liu, D. Kim, S. Kozlov, C. L. Stewart, and B. Burke (2009)
PNAS 106, 2194-2199
   Abstract »    Full Text »    PDF »
The lamin B receptor under transcriptional control of C/EBP{varepsilon} is required for morphological but not functional maturation of neutrophils.
T. V. Cohen, K. D. Klarmann, K. Sakchaisri, J. P. Cooper, D. Kuhns, M. Anver, P. F. Johnson, S. C. Williams, J. R. Keller, and C. L. Stewart (2008)
Hum. Mol. Genet. 17, 2921-2933
   Abstract »    Full Text »    PDF »
IMPa-4, an Arabidopsis Importin {alpha} Isoform, Is Preferentially Involved in Agrobacterium-Mediated Plant Transformation.
S. Bhattacharjee, L.-Y. Lee, H. Oltmanns, H. Cao, Veena, J. Cuperus, and S. B. Gelvin (2008)
PLANT CELL 20, 2661-2680
   Abstract »    Full Text »    PDF »
Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation.
D. J. Anderson and M. W. Hetzer (2008)
J. Cell Biol. 182, 911-924
   Abstract »    Full Text »    PDF »
Tissue-Specific Defects Are Caused by Loss of the Drosophila MAN1 LEM Domain Protein.
B. S. Pinto, S. R. Wilmington, E. E. L. Hornick, L. L. Wallrath, and P. K. Geyer (2008)
Genetics 180, 133-145
   Abstract »    Full Text »    PDF »
Effects of Lamin A/C, Lamin B1, and Viral US3 Kinase Activity on Viral Infectivity, Virion Egress, and the Targeting of Herpes Simplex Virus UL34-Encoded Protein to the Inner Nuclear Membrane.
F. Mou, E. G. Wills, R. Park, and J. D. Baines (2008)
J. Virol. 82, 8094-8104
   Abstract »    Full Text »    PDF »
Apoptosis leads to a degradation of vital components of active nuclear transport and a dissociation of the nuclear lamina.
A. Kramer, I. Liashkovich, H. Oberleithner, S. Ludwig, I. Mazur, and V. Shahin (2008)
PNAS 105, 11236-11241
   Abstract »    Full Text »    PDF »
Emerin and the Nuclear Lamina in Muscle and Cardiac Disease.
J. M. Holaska (2008)
Circ. Res. 103, 16-23
   Abstract »    Full Text »    PDF »
Nuclear pore complex proteins mark the implantation window in human endometrium.
E. Guffanti, N. Kittur, Z. N. Brodt, A. J. Polotsky, S. M. Kuokkanen, D. S. Heller, S. L. Young, N. Santoro, and U. T. Meier (2008)
J. Cell Sci. 121, 2037-2045
   Abstract »    Full Text »    PDF »
Nuclear Shape, Mechanics, and Mechanotransduction.
K. N. Dahl, A. J.S. Ribeiro, and J. Lammerding (2008)
Circ. Res. 102, 1307-1318
   Abstract »    Full Text »    PDF »
Toward a High-Resolution View of Nuclear Dynamics.
L. Trinkle-Mulcahy and A. I. Lamond (2007)
Science 318, 1402-1407
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)