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Epithelial Protein Lost in Neoplasm, EPLIN, the Cellular and Molecular Prospects in Cancers

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Epithelial Protein Lost in Neoplasm, EPLIN, the Cellular and Molecular Prospects in Cancers biomolecules Review Epithelial Protein Lost in Neoplasm, EPLIN, the Cellular and Molecular Prospects in Cancers Jianyuan Zeng , Wen G. Jiang * and Andrew J. Sanders * Cardiff China Medical Research Collaborative (CCMRC), Division of Cancer and Genetics (DCG), Cardiff University School of Medicine, Henry Wellcome Building, Cardiff CF14 4XN, UK; [email protected] * Correspondence: [email protected] (W.G.J.); [email protected] (A.J.S.) Abstract: Epithelial Protein Lost In Neoplasm (EPLIN), also known as LIMA1 (LIM Domain And Actin Binding 1), was first discovered as a protein differentially expressed in normal and cancerous cell lines. It is now known to be key to the progression and metastasis of certain solid tumours. Despite a slow pace in understanding the biological role in cells and body systems, as well as its clinical implications in the early years since its discovery, recent years have witnessed a rapid progress in understanding the mechanisms of this protein in cells, diseases and indeed the body. EPLIN has drawn more attention over the past few years with its roles expanding from cell migration and cytoskeletal dynamics, to cell cycle, gene regulation, angiogenesis/lymphangiogenesis and lipid metabolism. This concise review summarises and discusses the recent progress in understanding EPLIN in biological processes and its implications in cancer. Keywords: EPLIN; molecular signalling; interactive partners; cancer progression Citation: Zeng, J.; Jiang, W.G.; 1. EPLIN, the Structure and Cellular Functions Sanders, A.J. Epithelial Protein Lost Epithelial Protein Lost In Neoplasm (EPLIN), also known as LIMA1 (LIM Domain in Neoplasm, EPLIN, the Cellular and And Actin Binding 1), was first reported some twenty years ago by Chang et al., as a Molecular Prospects in Cancers. differentially expressed protein in normal and cancerous cell lines, including keratinocyte Biomolecules 2021, 11, 1038. https:// cell lines HNOK and HOK18L [1]. It has since been implicated in the control of cancer doi.org/10.3390/biom11071038 cells and the progression of certain solid tumours. Despite a slow pace in understanding the biological role in cells and body systems and clinical implications in the early years Academic Editor: Q. Ping Dou following its discovery, more recently, rapid progress has been made in the mechanistic understanding of this protein in cells, the body and in a wider context of human tumours, Received: 7 June 2021 as summarised in past review articles by Collins et al. and Wu et al. [2,3]. EPLIN has Accepted: 13 July 2021 Published: 16 July 2021 drawn increased attention over the past few years, with its roles expanding from those initially indicated in cell migration and cytoskeletal dynamics to cell cycle, gene regulation, Publisher’s Note: MDPI stays neutral angiogenesis/lymphangiogenesis and lipid metabolism. This concise review summarises with regard to jurisdictional claims in and discusses the most recent progress in understanding EPLIN in biological processes published maps and institutional affil- and its implications in cancer. iations. EPLIN (Epithelial Protein Lost In Neoplasm) is present as two isoforms, a 600aa EPLIN-α and EPLIN-β. which has an additional 160aa at the amino terminus [4], and is generated from two distinct promoters [5]. A centrally located LIM Domain [4] and two actin binding sites, that flank on each side of it, allow EPLIN to gain the ability to bundle actin filaments [6] (Figure1). EPLIN has previously been shown to inhibit Copyright: © 2021 by the authors. Licensee MDPI, Basel, Switzerland. branching nucleation through Actin-related protein 2/3 (Arp2/3), hence EPLIN is able This article is an open access article to regulate actin dynamics [7]. Additionally, EPLIN was revealed to be a regulator to distributed under the terms and sustain adherens junctions (AJ), as it was directly linked to the cadherin–catenin complex conditions of the Creative Commons via α-catenin [6]. Downregulation or phosphorylation of EPLIN by extracellular signal- Attribution (CC BY) license (https:// regulated kinase (ERK) [8] can lead to disorganisation of the cytoskeleton, disassembly creativecommons.org/licenses/by/ of the cadherin–catenin complex, activation of the Wnt-catenin signalling pathway and 4.0/). expressional alterations in a range of elements such as diminishment of E-cadherin and Biomolecules 2021, 11, 1038. https://doi.org/10.3390/biom11071038 https://www.mdpi.com/journal/biomolecules Biomolecules 2021, 11, x FOR PEER REVIEW 2 of 15 Biomolecules 2021, 11, 1038 2 of 15 the cadherin–catenin complex, activation of the Wnt-catenin signalling pathway and expressional alterations in a range of elements such as diminishment of E-cadherin and upregulationupregulation ofof ZEB1-promotingZEB1-promoting Epithelial-MesenchymalEpithelial-Mesenchymal Transition Transition ( (EMT)EMT) [6,9 [6,9].]. This This allowsallows epithelialepithelial cellscells to to lose lose cell–cell cell–cell adhesion adhesion and and apical apical basal basal polarity, polarity and, and hence hence reor- ganisereorganise their their own structureown structure leading leading to mesenchymal to mesenchymal characteristics characteristics in order in to order gain invasiveto gain potential.invasive potential. Zhitnyak Zhitnyak et al. [10] et elucidated al. [10] thatelucidated disorganisation that disorganisation of the actin of cytoskeleton the actin andcytoskeleton E-cadherin-based and E-cadherin AJs occur-based during AJs occur earlier during stages earlier of Epidermal stages of Growth Epidermal Factor Growt (EGF)-h inducedFactor (EGF EMT)-induced in epithelial EMT IAR-20 in epithelial cells. The IAR disorganisation-20 cells. The disorganisation is essential for is the essential entire EMT for process,the entire which EMT leadsprocess to,loss which of cell–cellleads to loss contact. of cell It– iscell interesting contact. It to is note interesting that the to expression note that ofthe E-cadherin expression remains of E-cadherin unchanged remains despite unchanged the loss of despite cell–cell the adhesion. loss of cell During–cell theseadhesion. early eventsDuring of these EGF-induced early events EMT, of disruptionEGF-induced of colocalisationEMT, disruption between of colocalisation EPLIN and between linear AJ andEPLIN phosphorylation and linear AJ ofand EPLIN phosphorylation is observed, of which EPLIN remains is observed, in line which with remains earlier work in line by Zhangwith earlier et al. [work9–11] .by These Zhang findings et al. [9 indicate–11]. These that findings EPLIN contributesindicate that to EPLIN the progression contributes of EMTto the by progression at least disrupting of EMT theby at cell–cell least disrupting adhesion complex,the cell–cell which adhesion further complex, induces which metas- tasis.further Interestingly, induces metastasis. EPLIN wasInterestingly, found to EPLIN be essential was found for cell to divisionbe essential [12 ,for13]; cell EPLIN division was detected[12,13]; EPLIN to locate was at detected the cleavage to locate furrow at andthe cleavage to associate furrow myosin and IIto and associate Sept2 duringmyosin theII ingressionand Sept2 period.during the Recruitment ingression andperiod. accumulation Recruitment of and actin, accumulation myosin II, RhoAof actin, and myosin Cdc42 wereII, RhoA impacted and duringCdc42 late-stagewere impacted cytokinesis during following late-stage EPLIN cytokinesis depletion. following In addition, EPLIN loss ofdepletion. EPLIN led In toaddition, multinucleation, loss of EPLIN which led results to multinuclea in cytokinesistion, failurewhich [results12]. Further in cytokinesis study by Sundvoldfailure [12]. et al.,Further also emphasisedstudy by Sundvold the role EPLINet al., also plays emphasised in this key eventthe role of cellEPLIN proliferation, plays in bythis showing key event that of EPLIN cell proliferation, recruits Arv1 by (ACAT-related showing that proteinEPLIN requiredrecruits Arv1 for viability (ACAT 1),-related which supportsprotein required the efficient for viability progression 1), which of cell supp divisionorts the [13 ].efficient Collectively, progression these studiesof cell division suggest that[13]. EPLIN Collectively, is needed these for studies cytokinesis suggest and that crucial EPLIN for is recruitment needed for ofcytokinesis a number and of essential crucial elementsfor recruitment during of this a number process. of Theessential loss ofelements EPLIN during could leadthis process. to failure The of thisloss importantof EPLIN event,could enhancinglead to failure the of possibility this important of genetic event, instability enhancing and the contributingpossibility of togenetic carcinogenesis. instability and contributing to carcinogenesis. FigureFigure 1. 1.Schematic Schematic structure structure of of EPLIN. EPLIN Structural. Structural information information is is adapted adapted from from [5 ,[5,66] and] and figure figure is is designed designed and and created created by by using Adobe Illustrator 2021Version 25.2.1 (Adobe Inc., San Jose, CA, USA). using Adobe Illustrator 2021Version 25.2.1 (Adobe Inc., San Jose, CA, USA). 2. New Members of EPLIN’s Interacting/Regulatory Network 2. New Members of EPLIN’s Interacting/Regulatory Network To achieve EPLIN’s distinct functions in cellular events and metastatic progression, To achieve EPLIN’s distinct functions in cellular events and metastatic progression, a a number of interacting/regulatory partners are involved. As discussed above and number of interacting/regulatory
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