The nuclear lamins: flexibility in function
B Burke, CL Stewart - Nature reviews Molecular cell biology, 2013 - nature.com
The nuclear lamina is an important structural determinant for the nuclear envelope as a
whole, attaching chromatin domains to the nuclear periphery and localizing some nuclear …
whole, attaching chromatin domains to the nuclear periphery and localizing some nuclear …
Accessorizing and anchoring the LINC complex for multifunctionality
W Chang, HJ Worman, GG Gundersen - Journal of Cell Biology, 2015 - rupress.org
The linker of nucleoskeleton and cytoskeleton (LINC) complex, composed of outer and inner
nuclear membrane Klarsicht, ANC-1, and Syne homology (KASH) and Sad1 and UNC-84 …
nuclear membrane Klarsicht, ANC-1, and Syne homology (KASH) and Sad1 and UNC-84 …
Coupling of the nucleus and cytoplasm: role of the LINC complex
M Crisp, Q Liu, K Roux, JB Rattner… - The Journal of cell …, 2006 - rupress.org
The nuclear envelope defines the barrier between the nucleus and cytoplasm and features
inner and outer membranes separated by a perinuclear space (PNS). The inner nuclear …
inner and outer membranes separated by a perinuclear space (PNS). The inner nuclear …
LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins
BA Sosa, A Rothballer, U Kutay, TU Schwartz - Cell, 2012 - cell.com
Linker of nucleoskeleton and cytoskeleton (LINC) complexes span the nuclear envelope
and are composed of KASH and SUN proteins residing in the outer and inner nuclear …
and are composed of KASH and SUN proteins residing in the outer and inner nuclear …
Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges
DA Starr, HN Fridolfsson - Annual review of cell and …, 2010 - annualreviews.org
The nuclear envelope links the cytoskeleton to structural components of the nucleus. It
functions to coordinate nuclear migration and anchorage, organize chromatin, and aid …
functions to coordinate nuclear migration and anchorage, organize chromatin, and aid …
The nuclear lamina comes of age
Y Gruenbaum, A Margalit, RD Goldman… - … reviews Molecular cell …, 2005 - nature.com
Many nuclear proteins form lamin-dependent complexes, including LEM-domain proteins,
nesprins and SUN-domain proteins. These complexes have roles in chromatin organization …
nesprins and SUN-domain proteins. These complexes have roles in chromatin organization …
SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton
F Haque, DJ Lloyd, DT Smallwood… - … and cellular biology, 2006 - Taylor & Francis
Nuclear migration and positioning within cells are critical for many developmental processes
and are governed by the cytoskeletal network. Although mechanisms of nuclear-cytoskeletal …
and are governed by the cytoskeletal network. Although mechanisms of nuclear-cytoskeletal …
Nuclear lamins: laminopathies and their role in premature ageing
It has been demonstrated that nuclear lamins are important proteins in maintaining cellular
as well as nuclear integrity, and in maintaining chromatin organization in the nucleus …
as well as nuclear integrity, and in maintaining chromatin organization in the nucleus …
The nuclear envelope lamina network has elasticity and a compressibility limit suggestive of a molecular shock absorber
Mechanical properties of the nuclear envelope have implications for cell and nuclear
architecture as well as gene regulation. Using isolated Xenopus oocyte nuclei, we have …
architecture as well as gene regulation. Using isolated Xenopus oocyte nuclei, we have …
Nesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization
KJ Roux, ML Crisp, Q Liu, D Kim… - Proceedings of the …, 2009 - National Acad Sciences
Nucleocytoplasmic coupling is mediated by outer nuclear membrane (ONM) nesprin
proteins and inner nuclear membrane Sun proteins. Interactions spanning the perinuclear …
proteins and inner nuclear membrane Sun proteins. Interactions spanning the perinuclear …