Literature DB >> 8557486

The dynamic properties and possible functions of nuclear lamins.

R D Moir1, T P Spann, R D Goldman.   

Abstract

The nuclear lamins are thought to form a thin fibrous layer called the nuclear lamina, underlying the inner nuclear envelope membrane. In this review, we summarize data on the dynamic properties of nuclear lamins during the cell cycle and during development. We discuss the implications of dynamics for lamin functions. The lamins may be involved in DNA replication, chromatin organization, differentiation, nuclear structural support, and nuclear envelope reassembly. Emphasis is placed on recent data that indicate that the lamina, contrary to previous views, is not a static structure. For example, the lamins form nucleoplasmic foci, distinct from the peripheral lamina, which vary in their patterns of distribution as well as their composition in a cell cycle-dependent manner. During the S phase, these foci colocalize with chromatin and sites of DNA replication. At other points during the cell cycle, they may represent sites of lamin post-translation processing that take place prior to incorporation into the lamina. Secondary modifications of the lamins such as isoprenylation and phosphorylation are involved in the regulation of the dynamic properties and the assembly of lamins. In addition, a number of lamin-associated proteins have been recently identified and these are described along with their potential functions.

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Year:  1995        PMID: 8557486     DOI: 10.1016/s0074-7696(08)62616-9

Source DB:  PubMed          Journal:  Int Rev Cytol        ISSN: 0074-7696


  44 in total

1.  The tail domain of lamin Dm0 binds histones H2A and H2B.

Authors:  M Goldberg; A Harel; M Brandeis; T Rechsteiner; T J Richmond; A M Weiss; Y Gruenbaum
Journal:  Proc Natl Acad Sci U S A       Date:  1999-03-16       Impact factor: 11.205

2.  Meiotic lamin C2: the unique amino-terminal hexapeptide GNAEGR is essential for nuclear envelope association.

Authors:  M Alsheimer; E von Glasenapp; M Schnolzer; H Heid; R Benavente
Journal:  Proc Natl Acad Sci U S A       Date:  2000-11-21       Impact factor: 11.205

3.  REST/NRSF-interacting LIM domain protein, a putative nuclear translocation receptor.

Authors:  Masahito Shimojo; Louis B Hersh
Journal:  Mol Cell Biol       Date:  2003-12       Impact factor: 4.272

4.  The presenilins turned inside out: implications for their structures and functions.

Authors:  Nazneen N Dewji; Dante Valdez; S J Singer
Journal:  Proc Natl Acad Sci U S A       Date:  2004-01-19       Impact factor: 11.205

5.  Nuclear envelope irregularity is induced by RET/PTC during interphase.

Authors:  Andrew H Fischer; Panya Taysavang; Sissy M Jhiang
Journal:  Am J Pathol       Date:  2003-09       Impact factor: 4.307

6.  Nucleoskeleton of early bovine embryos and differentiated somatic cells: an ultrastructural and immunocytochemical comparison.

Authors:  Jéril Degrouard; Pavel Hozák; Yvan Heyman; Jacques-Edmond Fléchon
Journal:  Histochem Cell Biol       Date:  2004-05-25       Impact factor: 4.304

7.  Molecular diversity of rat brain proteins as revealed by proteomic analysis.

Authors:  Jae-Won Yang; Jean-François Juranville; Harald Höger; Michael Fountoulakis; Gert Lubec
Journal:  Mol Divers       Date:  2005       Impact factor: 2.943

8.  Interaction of bovine papillomavirus E2 protein with Brd4 stabilizes its association with chromatin.

Authors:  Maria G McPhillips; Keiko Ozato; Alison A McBride
Journal:  J Virol       Date:  2005-07       Impact factor: 5.103

9.  Power-law rheology of isolated nuclei with deformation mapping of nuclear substructures.

Authors:  Kris Noel Dahl; Adam J Engler; J David Pajerowski; Dennis E Discher
Journal:  Biophys J       Date:  2005-07-29       Impact factor: 4.033

10.  Epstein-Barr virus BGLF4 kinase induces disassembly of the nuclear lamina to facilitate virion production.

Authors:  Chung-Pei Lee; Yu-Hao Huang; Su-Fang Lin; Yao Chang; Yu-Hsin Chang; Kenzo Takada; Mei-Ru Chen
Journal:  J Virol       Date:  2008-09-24       Impact factor: 5.103

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