Skeletal Muscle Dystrophy mutant of lamin A alters the structure and dynamics of the Ig fold domain View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2018-12

AUTHORS

Subarna Dutta, Jitendra K. Das, Lakshmi Maganti, Maitree Bhattacharyya, Dhananjay Bhattacharyya, Sujoy Mukherjee, Kaushik Sengupta

ABSTRACT

Mutations in the different domains of A-type lamin proteins cause a diverse plethora of diseases collectively termed as laminopathies which can affect multiple organs. Ig fold is one such domain of lamin A which is implicated in numerous nuclear interactions wherein the mutations lead to different laminopathies. W514R is one such mutation in the Ig fold which leads to severe phenotypes in Skeletal Muscle Dystrophy (SMD) which is a class of laminopathies. In this report, we elucidated gross alterations in structure and dynamics at the level of individual amino acids. These studies indicate altered conformational features of residues in the close vicinity of W514. Imaging of mammalian cells transfected with the mutant have shown distinct perturbation of the nuclear meshwork with concomitant alteration in nuclear interactions as a result of increased oligomerization of Ig W514R. Hence, this novel approach of amalgamating theoretical and experimental procedures to predict the severity of a mutant in the context of laminopathies could be extended for numerous lamin A mutants. More... »

PAGES

13793

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41598-018-32227-2

DOI

http://dx.doi.org/10.1038/s41598-018-32227-2

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1106921321

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30218058


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