Literature DB >> 10806083

Review: the dynamics of the nuclear lamins during the cell cycle-- relationship between structure and function.

R D Moir1, T P Spann, R I Lopez-Soler, M Yoon, A E Goldman, S Khuon, R D Goldman.   

Abstract

The nuclear lamins are members of the intermediate filament (IF) family of proteins. The lamins have an essential role in maintaining nuclear integrity, as do the other IF family members in the cytoplasm. Also like cytoplasmic IFs, the organization of lamins is dynamic. The lamins are found not only at the nuclear periphery but also in the interior of the nucleus, as distinct nucleoplasmic foci and possibly as a network throughout the nucleus. Nuclear processes such as DNA replication may be organized around these structures. In this review, we discuss changes in the structure and organization of the nuclear lamins during the cell cycle and during cell differentiation. These changes are correlated with changes in nuclear structure and function. For example, the interactions of lamins with chromatin and nuclear envelope components occur very early during nuclear assembly following mitosis. During S-phase, the lamins colocalize with markers of DNA replication, and proper lamin organization must be maintained for replication to proceed. When cells differentiate, the expression pattern of lamin isotypes changes. In addition, changes in lamin organization and expression patterns accompany the nuclear alterations observed in transformed cells. These lamin structures may modulate nuclear function in each of these processes. Copyright 2000 Academic Press.

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Year:  2000        PMID: 10806083     DOI: 10.1006/jsbi.2000.4251

Source DB:  PubMed          Journal:  J Struct Biol        ISSN: 1047-8477            Impact factor:   2.867


  35 in total

1.  Nuclear organization of DNA replication in primary mammalian cells.

Authors:  B K Kennedy; D A Barbie; M Classon; N Dyson; E Harlow
Journal:  Genes Dev       Date:  2000-11-15       Impact factor: 11.361

2.  Localization of importin alpha (Rch1) at the plasma membrane and subcellular redistribution during lymphocyte activation.

Authors:  Ricardo Andrade; Raúl Alonso; Raúl Peña; Jon Arlucea; Juan Aréchaga
Journal:  Chromosoma       Date:  2003-07-15       Impact factor: 4.316

3.  Investigation of differentially expressed proteins in rat gastrocnemius muscle during denervation-reinnervation.

Authors:  Hualin Sun; Jie Liu; Fei Ding; Xiaodong Wang; Mei Liu; Xiaosong Gu
Journal:  J Muscle Res Cell Motil       Date:  2006-06-04       Impact factor: 2.698

4.  Laminopathic mutations interfere with the assembly, localization, and dynamics of nuclear lamins.

Authors:  Naama Wiesel; Anna Mattout; Shai Melcer; Naomi Melamed-Book; Harald Herrmann; Ohad Medalia; Ueli Aebi; Yosef Gruenbaum
Journal:  Proc Natl Acad Sci U S A       Date:  2007-12-27       Impact factor: 11.205

Review 5.  Nuclear lamins: major factors in the structural organization and function of the nucleus and chromatin.

Authors:  Thomas Dechat; Katrin Pfleghaar; Kaushik Sengupta; Takeshi Shimi; Dale K Shumaker; Liliana Solimando; Robert D Goldman
Journal:  Genes Dev       Date:  2008-04-01       Impact factor: 11.361

Review 6.  Nuclear mechanics in cancer.

Authors:  Celine Denais; Jan Lammerding
Journal:  Adv Exp Med Biol       Date:  2014       Impact factor: 2.622

7.  Fibroblasts lacking nuclear lamins do not have nuclear blebs or protrusions but nevertheless have frequent nuclear membrane ruptures.

Authors:  Natalie Y Chen; Paul Kim; Thomas A Weston; Lovelyn Edillo; Yiping Tu; Loren G Fong; Stephen G Young
Journal:  Proc Natl Acad Sci U S A       Date:  2018-09-17       Impact factor: 11.205

8.  Do lamin B1 and lamin B2 have redundant functions?

Authors:  John M Lee; Hea-Jin Jung; Loren G Fong; Stephen G Young
Journal:  Nucleus       Date:  2014 Jul-Aug       Impact factor: 4.197

9.  The role of transcription factories-mediated interchromosomal contacts in the organization of nuclear architecture.

Authors:  Julien Dorier; Andrzej Stasiak
Journal:  Nucleic Acids Res       Date:  2010-07-31       Impact factor: 16.971

10.  Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner.

Authors:  Nathalie Britzen-Laurent; Michael Bauer; Valeria Berton; Nicole Fischer; Adrian Syguda; Simone Reipschläger; Elisabeth Naschberger; Christian Herrmann; Michael Stürzl
Journal:  PLoS One       Date:  2010-12-07       Impact factor: 3.240

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