Literature DB >> 36205821

The role of inner nuclear membrane proteins in tumourigenesis and as potential targets for cancer therapy.

Maddison Rose1, Joshua T Burgess1, Kenneth O'Byrne1,2, Derek J Richard1, Emma Bolderson3.   

Abstract

Despite significant advances in our understanding of tumourigenesis and cancer therapeutics, cancer continues to account for 30% of worldwide deaths. Therefore, there remains an unmet need for the development of cancer therapies to improve patient quality of life and survival outcomes. The inner nuclear membrane has an essential role in cell division, cell signalling, transcription, cell cycle progression, chromosome tethering, cell migration and mitosis. Furthermore, expression of several inner nuclear membrane proteins has been shown to be frequently altered in tumour cells, resulting in the dysregulation of cellular pathways to promote tumourigenesis. However, to date, minimal research has been conducted to investigate how targeting these dysregulated and variably expressed proteins may provide a novel avenue for cancer therapies. In this review, we present an overview of the involvement of the inner nuclear membrane proteins within the hallmarks of cancer and how they may be exploited as potent anti-cancer therapeutics.
© 2022. The Author(s).

Entities:  

Keywords:  Banf1; Cancer; Cancer therapeutics; Lamin; Lem-Domain protein; Nuclear envelope

Year:  2022        PMID: 36205821     DOI: 10.1007/s10555-022-10065-z

Source DB:  PubMed          Journal:  Cancer Metastasis Rev        ISSN: 0167-7659            Impact factor:   9.237


  83 in total

1.  A phosphorylation cluster in the chromatin-binding region regulates chromosome association of LAP2alpha.

Authors:  Andreas Gajewski; Edina Csaszar; Roland Foisner
Journal:  J Biol Chem       Date:  2004-06-18       Impact factor: 5.157

Review 2.  Making the LINC: SUN and KASH protein interactions.

Authors:  Dae In Kim; K C Birendra; Kyle J Roux
Journal:  Biol Chem       Date:  2015-04       Impact factor: 3.915

Review 3.  The mitotic spindle matrix: a fibro-membranous lamin connection.

Authors:  Yixian Zheng; Ming-Ying Tsai
Journal:  Cell Cycle       Date:  2006-10-16       Impact factor: 4.534

4.  Cell-cycle-dependent phosphorylation of the nuclear pore Nup107-160 subcomplex.

Authors:  Joseph S Glavy; Andrew N Krutchinsky; Ileana M Cristea; Ian C Berke; Thomas Boehmer; Günter Blobel; Brian T Chait
Journal:  Proc Natl Acad Sci U S A       Date:  2007-02-28       Impact factor: 11.205

5.  Phosphorylation of Nup98 by multiple kinases is crucial for NPC disassembly during mitotic entry.

Authors:  Eva Laurell; Katja Beck; Ksenia Krupina; Gandhi Theerthagiri; Bernd Bodenmiller; Peter Horvath; Ruedi Aebersold; Wolfram Antonin; Ulrike Kutay
Journal:  Cell       Date:  2011-02-18       Impact factor: 41.582

6.  In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase.

Authors:  M Peter; J Nakagawa; M Dorée; J C Labbé; E A Nigg
Journal:  Cell       Date:  1990-05-18       Impact factor: 41.582

Review 7.  Anti-cancer therapy made easier: a 25-year update.

Authors:  Amy Davies; Caroline Lum; Rachel Raju; Evan Ansell; Kate Webber; Eva Segelov
Journal:  Intern Med J       Date:  2021-04       Impact factor: 2.048

Review 8.  Innovation in cancer therapeutics and regulatory perspectives.

Authors:  Pinky Sharma; Vikas Jhawat; Pooja Mathur; Rohit Dutt
Journal:  Med Oncol       Date:  2022-02-23       Impact factor: 3.738

9.  LEM-4 promotes rapid dephosphorylation of BAF during mitotic exit.

Authors:  Mátyás Gorjánácz
Journal:  Nucleus       Date:  2012-12-04       Impact factor: 4.197

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