Literature DB >> 32413188

Genotype-phenotype analysis of LMNA-related diseases predicts phenotype-selective alterations in lamin phosphorylation.

Eric W Lin1,2, Graham F Brady1,2, Raymond Kwan1,3, Alexey I Nesvizhskii4,5, M Bishr Omary1,2,3.   

Abstract

Laminopathies are rare diseases associated with mutations in LMNA, which encodes nuclear lamin A/C. LMNA variants lead to diverse tissue-specific phenotypes including cardiomyopathy, lipodystrophy, myopathy, neuropathy, progeria, bone/skin disorders, and overlap syndromes. The mechanisms underlying these heterogeneous phenotypes remain poorly understood, although post-translational modifications, including phosphorylation, are postulated as regulators of lamin function. We catalogued all known lamin A/C human mutations and their associated phenotypes, and systematically examined the putative role of phosphorylation in laminopathies. In silico prediction of specific LMNA mutant-driven changes to lamin A phosphorylation and protein structure was performed using machine learning methods. Some of the predictions we generated were validated via assessment of ectopically expressed wild-type and mutant LMNA. Our findings indicate phenotype- and mutant-specific alterations in lamin phosphorylation, and that some changes in phosphorylation may occur independently of predicted changes in lamin protein structure. Therefore, therapeutic targeting of phosphorylation in the context of laminopathies will likely require mutant- and kinase-specific approaches.
© 2020 Federation of American Societies for Experimental Biology.

Entities:  

Keywords:  intermediate filaments; laminopathy; mutation; post-translational modifications

Mesh:

Substances:

Year:  2020        PMID: 32413188      PMCID: PMC8059629          DOI: 10.1096/fj.202000500R

Source DB:  PubMed          Journal:  FASEB J        ISSN: 0892-6638            Impact factor:   5.191


  69 in total

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Journal:  Annu Rev Biochem       Date:  2004       Impact factor: 23.643

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

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Review 3.  Intermediate Filaments: Structure and Assembly.

Authors:  Harald Herrmann; Ueli Aebi
Journal:  Cold Spring Harb Perspect Biol       Date:  2016-11-01       Impact factor: 10.005

4.  The defective nuclear lamina in Hutchinson-gilford progeria syndrome disrupts the nucleocytoplasmic Ran gradient and inhibits nuclear localization of Ubc9.

Authors:  Joshua B Kelley; Sutirtha Datta; Chelsi J Snow; Mandovi Chatterjee; Li Ni; Adam Spencer; Chun-Song Yang; Caelin Cubeñas-Potts; Michael J Matunis; Bryce M Paschal
Journal:  Mol Cell Biol       Date:  2011-06-13       Impact factor: 4.272

5.  Chemical chaperone therapy, a new strategy for genetic skin fragility disorders.

Authors:  Jean Christopher Chamcheu; Imtiaz A Siddiqui; Hasan Mukhtar
Journal:  Exp Dermatol       Date:  2016-03       Impact factor: 3.960

Review 6.  Post-translational modifications of intermediate filament proteins: mechanisms and functions.

Authors:  Natasha T Snider; M Bishr Omary
Journal:  Nat Rev Mol Cell Biol       Date:  2014-03       Impact factor: 94.444

7.  Mitogen-activated protein kinase kinase 1/2 inhibition and angiotensin II converting inhibition in mice with cardiomyopathy caused by lamin A/C gene mutation.

Authors:  Antoine Muchir; Wei Wu; Fusako Sera; Shunichi Homma; Howard J Worman
Journal:  Biochem Biophys Res Commun       Date:  2014-09-11       Impact factor: 3.575

8.  Phospho.ELM: a database of phosphorylation sites--update 2011.

Authors:  Holger Dinkel; Claudia Chica; Allegra Via; Cathryn M Gould; Lars J Jensen; Toby J Gibson; Francesca Diella
Journal:  Nucleic Acids Res       Date:  2010-11-09       Impact factor: 16.971

9.  Significance of 1B and 2B domains in modulating elastic properties of lamin A.

Authors:  Manindra Bera; Sri Rama Koti Ainavarapu; Kaushik Sengupta
Journal:  Sci Rep       Date:  2016-06-15       Impact factor: 4.379

10.  DynaMut: predicting the impact of mutations on protein conformation, flexibility and stability.

Authors:  Carlos Hm Rodrigues; Douglas Ev Pires; David B Ascher
Journal:  Nucleic Acids Res       Date:  2018-07-02       Impact factor: 16.971

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  5 in total

Review 1.  Post-Translational Modification of Lamins: Mechanisms and Functions.

Authors:  Mingyue Zheng; Guoxiang Jin; Zhongjun Zhou
Journal:  Front Cell Dev Biol       Date:  2022-05-17

2.  Nuclear lamin phosphorylation: an emerging role in gene regulation and pathogenesis of laminopathies.

Authors:  Sunny Yang Liu; Kohta Ikegami
Journal:  Nucleus       Date:  2020-12       Impact factor: 4.197

3.  A Transfer-Learning-Based Deep Convolutional Neural Network for Predicting Leukemia-Related Phosphorylation Sites from Protein Primary Sequences.

Authors:  Jian He; Yanling Wu; Xuemei Pu; Menglong Li; Yanzhi Guo
Journal:  Int J Mol Sci       Date:  2022-02-03       Impact factor: 5.923

Review 4.  Current and Future Approaches to Classify VUSs in LGMD-Related Genes.

Authors:  Chengcheng Li; Gabe Haller; Conrad C Weihl
Journal:  Genes (Basel)       Date:  2022-02-19       Impact factor: 4.096

5.  Tyrosine phosphorylation of lamin A by Src promotes disassembly of nuclear lamina in interphase.

Authors:  Ching-Tung Chu; Yi-Hsuan Chen; Wen-Tai Chiu; Hong-Chen Chen
Journal:  Life Sci Alliance       Date:  2021-08-12
  5 in total

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