4.6 Article

Lamin complexes in the nuclear interior control progenitor cell proliferation and tissue homeostasis

期刊

CELL CYCLE
卷 8, 期 10, 页码 1488-1493

出版社

TAYLOR & FRANCIS INC
DOI: 10.4161/cc.8.10.8499

关键词

cell cycle control; nucleoplasmic lamins; LAP2; tissue progenitor cells; laminopathies; retinoblastoma

资金

  1. Austrian Science Research Fund [P17871]
  2. European Commission [LSHM-CT-2005-018690]
  3. Austrian Science Fund (FWF) [P17871] Funding Source: Austrian Science Fund (FWF)

向作者/读者索取更多资源

Lamins are components of the peripheral nuclear lamina that has important mechanical roles in nuclear architecture. Lamins have increasingly been implicated in nuclear processes, including DNA replication, chromatin organization and transcription. Recent data highlight the specific functions of a small pool of lamina-independent A-type lamins, located throughout the nucleoplasm, in the regulation of cell cycle progression in early tissue progenitor cells. This novel role of nucleoplasmic lamins is likely mediated by their regulatory activity towards the tumor suppressor Retinoblastoma protein. We describe how an interaction partner of A-type lamins, lamina-associated polypeptide 2 alpha (LAP2 alpha) affects targeting of lamins A and C to the nuclear interior and how this complex may affect cell cycle progression and tissue homeostasis. Finally, we discuss implications of these novel findings for understanding the pathogenesis of laminopathies, a group of human diseases caused by mutations in lamins.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.6
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

Article Oncology

Barrier-to-Autointegration Factor (BAF) involvement in prelamin A-related chromatin organization changes

Manuela Loi, Vittoria Cenni, Serena Duchi, Stefano Squarzoni, Carlos Lopez-Otin, Roland Foisner, Giovanna Lattanzi, Cristina Capanni

ONCOTARGET (2016)

Article Biochemistry & Molecular Biology

A-type lamins bind both hetero- and euchromatin, the latter being regulated by lamina-associated polypeptide 2 alpha

Kevin Gesson, Philipp Rescheneder, Michael P. Skoruppa, Arndt von Haeseler, Thomas Dechat, Roland Foisner

GENOME RESEARCH (2016)

Review Cell Biology

Molecular insights into the premature aging disease progeria

Sandra Vidak, Roland Foisner

HISTOCHEMISTRY AND CELL BIOLOGY (2016)

Article Cell Biology

Cdc48 and Ubx1 participate in a pathway associated with the inner nuclear membrane that governs Asi1 degradation

Marina Pantazopoulou, Mirta Boban, Roland Foisner, Per O. Ljungdahl

JOURNAL OF CELL SCIENCE (2016)

Article Multidisciplinary Sciences

The GIY-YIG Type Endonuclease Ankyrin Repeat and LEM Domain-Containing Protein 1 (ANKLE1) Is Dispensable for Mouse Hematopoiesis

Juliane Braun, Arabella Meixner, Andreas Brachner, Roland Foisner

PLOS ONE (2016)

Review Cell Biology

Degradation-mediated protein quality control at the inner nuclear membrane

Mirta Boban, Roland Foisner

NUCLEUS (2016)

Review Cell Biology

Degradation-mediated protein quality control at the inner nuclear membrane

Mirta Boban, Roland Foisner

NUCLEUS (2016)

Article Cell Biology

Nucleoplasmic lamins define growth-regulating functions of lamina-associated polypeptide 2 alpha in progeria cells

Sandra Vidak, Konstantina Georgiou, Petra Fichtinger, Nana Naetar, Thomas Dechat, Roland Foisner

JOURNAL OF CELL SCIENCE (2018)

Editorial Material Cell Biology

Lamins in the nuclear interior - life outside the lamina

Nana Naetar, Simona Ferraioli, Roland Foisner

JOURNAL OF CELL SCIENCE (2017)

Article Cell Biology

Comparative Interactome Analysis of Emerin, MAN1 and LEM2 Reveals a Unique Role for LEM2 in Nucleotide Excision Repair

Bernhard Moser, Jose Basilio, Josef Gotzmann, Andreas Brachner, Roland Foisner

Article Biology

LAP2alpha maintains a mobile and low assembly state of A-type lamins in the nuclear interior

Nana Naetar, Konstantina Georgiou, Christian Knapp, Irena Bronshtein, Elisabeth Zier, Petra Fichtinger, Thomas Dechat, Yuval Garini, Roland Foisner

Summary: The loss of LAP2 alpha leads to the formation of larger, biochemically stable lamin A/C structures in the nuclear interior that are inaccessible to lamin A/C antibodies. Binding of LAP2 alpha to lamin A/C inhibits the formation of higher order structures, keeping nucleoplasmic lamin A/C in a mobile state. This suggests that LAP2 alpha is essential for maintaining a mobile lamin A/C pool in the nuclear interior, necessary for proper nuclear functions.
暂无数据