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Fused in sarcoma (FUS) interacts with the cytolinker protein plectin: implications for FUS subcellular localization and function.

Journal article
Authors Christer Thomsen
Sameer Udhane
Rikard Runnberg
Gerhard Wiche
Anders Ståhlberg
Pierre Åman
Published in Experimental cell research
Volume 318
Issue 5
Pages 653-61
ISSN 1090-2422
Publication year 2012
Published at Institute of Biomedicine, Department of Pathology
Pages 653-61
Language en
Links dx.doi.org/10.1016/j.yexcr.2011.12....
Keywords Animals, Cell Line, Cell Nucleus, metabolism, Cytoplasm, metabolism, Fibroblasts, metabolism, Gene Knockout Techniques, Humans, Mice, Plectin, chemistry, genetics, metabolism, Protein Binding, Protein Interaction Domains and Motifs, Protein Interaction Mapping, Protein Transport, RNA, Messenger, metabolism, RNA-Binding Protein FUS, chemistry, metabolism
Subject categories Basic Medicine

Abstract

Fused in sarcoma (FUS) is a multifunctional protein involved in transcriptional control, pre-mRNA processing, RNA transport and translation. The domain structure of FUS reflects its functions in gene regulation and its ability to interact with other proteins, RNA and DNA. By use of a recombinant fragment of FUS in pull-down experiments followed by mass spectrometry analysis we have identified a novel interaction between the FUS N-terminal and the cytolinker plectin. An in situ proximity ligation assay confirmed that FUS-plectin interactions take place in the cytoplasm of cells. Furthermore, plectin deficient cells showed an altered subcellular localization of FUS and a deregulated expression of mRNAs bound to FUS. Our results show that plectin is important for normal FUS localization and function. Mutations involving FUS are causative factors in sarcomas and leukemias and also hereditary forms of amyotrophic lateral sclerosis and frontotemporal lobar degeneration. Plectin deficiency causes epidermolysis bullosa, a disease involving the skin and neuromuscular system. The novel FUS-plectin interaction offers new perspectives for understanding the role of FUS and plectin mutations in the pathogenesis of these diseases.

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