α-Actinin links LPP, but not zyxin, to cadherin-based junctions

Hansen, Marc D.H.; Beckerle, Mary C.

doi:10.1016/j.bbrc.2008.04.018

Cited by 9 publications

(3 citation statements)

References 16 publications

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“…Thus, α-actinin may be part of a mechanotransduction mechanism for vinculin recruitment to the cadherin–catenin complex. Besides binding to α-catenin and vinculin, α-actinin also interacts with other junctional proteins, including ADIP ( Asada et al, 2003 ), LMO7 ( Ooshio et al, 2004 ), LPP ( Hansen and Beckerle, 2008 ), MAGI ( Patrie et al, 2002 ), and β-catenin ( Catimel et al, 2005 ; Gujral et al, 2013 ).…”

Section: Introductionmentioning

confidence: 99%

Synaptopodin couples epithelial contractility to α-actinin-4–dependent junction maturation

Kannan

Tang

2015

Journal of Cell Biology

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Section: Introductionmentioning

confidence: 99%

Synaptopodin couples epithelial contractility to α-actinin-4–dependent junction maturation

Kannan

Tang

2015

Journal of Cell Biology

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“…LPP may exert its pro-migratory effects via its ability to bind α-Actinin (Hansen and Beckerle, 2008; Li et al, 2003). We demonstrate that loss of α-Actinin binding to LPP has the same effect as the complete loss of LPP, suggesting that α-Actinin is the major downstream mediator through which LPP functions to enhance the migration and invasion of ErbB2 expressing breast cancer cells in response to TGFβ.…”

Section: Discussionmentioning

confidence: 99%

A complex containing LPP and α-Actinin mediates TGFβ-induced migration and invasion of ErbB2-expressing breast cancer cells

Ngan

Northey

Brown

et al. 2013

Journal of Cell Science

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SummaryTransforming growth factor b (TGFb) is a potent modifier of the malignant phenotype in ErbB2-expressing breast cancers. We demonstrate that epithelial-derived breast cancer cells, which undergo a TGFb-induced epithelial-to-mesenchymal transition (EMT), engage signaling molecules that normally facilitate cellular migration and invasion of mesenchymal cells. We identify lipoma preferred partner (LPP) as an indispensable regulator of TGFb-induced migration and invasion of ErbB2-expressing breast cancer cells. We show that LPP re-localizes to focal adhesion complexes upon TGFb stimulation and is a critical determinant in TGFb-mediated focal adhesion turnover. Finally, we have determined that the interaction between LPP and a-actinin, an actin cross-linking protein, is necessary for TGFb-induced migration and invasion of ErbB2-expressing breast cancer cells. Thus, our data reveal that LPP, which is normally operative in cells of mesenchymal origin, can be co-opted by breast cancer cells during an EMT to promote their migration and invasion.

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“…The molecular mechanisms underlying their recruitment to junctions have not been established and might be complex. Zyxin is recruited to tensile F-actin (Nguyen et al, 2010;Yoshigi et al, 2005), which is certainly present at cell-cell junctions, but the close Zyxin homologs Ajuba and lipoma preferred partner (LPP) are known to be recruited by a-catenin and a-actinin (Hansen and Beckerle, 2008;Marie et al, 2003), which are also present in mechanical force-chains. Moreover, Zyxin localization to cell-cell adhesions has recently been attributed to its interaction with nectin (Gregory Call et al, 2011).…”

Section: Zyxin and Vasp -Potential Cell-cell Mechanosensing Beyond VImentioning

confidence: 99%

Mechanosensitive systems at the cadherin–F-actin interface

Huveneers

Rooij

2013

Journal of Cell Science

201

189

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SummaryCells integrate biochemical and mechanical information to function within multicellular tissue. Within developing and remodeling tissues, mechanical forces contain instructive information that governs important cellular processes that include stem cell maintenance, differentiation and growth. Although the principles of signal transduction (protein phosphorylation, allosteric regulation of enzymatic activity and binding sites) are the same for biochemical and mechanical-induced signaling, the first step of mechanosensing, in which protein complexes under tension transduce changes in physical force into cellular signaling, is very different, and the molecular mechanisms are only beginning to be elucidated. In this Commentary, we focus on mechanotransduction at cell-cell junctions, aiming to comprehend the molecular mechanisms involved. We describe how different junction structures are associated with the actomyosin cytoskeleton and how this relates to the magnitude and direction of forces at cell-cell junctions. We discuss which cell-cell adhesion receptors have been shown to take part in mechanotransduction. Then we outline the force-induced molecular events that might occur within a key mechanosensitive system at cell-cell junctions; the cadherin-F-actin interface, at which a-catenin and vinculin form a central module. Mechanotransduction at cell-cell junctions emerges as an important signaling mechanism, and we present examples of its potential relevance for tissue development and disease.

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α-Actinin links LPP, but not zyxin, to cadherin-based junctions

Cited by 9 publications

References 16 publications

Synaptopodin couples epithelial contractility to α-actinin-4–dependent junction maturation

Synaptopodin couples epithelial contractility to α-actinin-4–dependent junction maturation

A complex containing LPP and α-Actinin mediates TGFβ-induced migration and invasion of ErbB2-expressing breast cancer cells

Mechanosensitive systems at the cadherin–F-actin interface

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