Emerging properties of adhesion complexes: what are they and what do they do?

Humphries, Jonathan D.; Paul, Nikki R.; Morgan, Mark R.

doi:10.1016/j.tcb.2015.02.008

Cited by 76 publications

(71 citation statements)

References 123 publications

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“…This could be achieved through regulating the activities of the respective pathways via tyrosine phosphorylation of the component proteins. Indeed, specific localization of mRNA and ribosomal proteins at adhesion sites or specialized cytoskeleton domains with a result of local protein translation have been repeatedly observed242526. Our observation indicates that the specific localization and/or activation of proteins involved in translation is probably regulated by tyrosine phosphorylation.…”

Section: Discussionsupporting

confidence: 61%

Quantitative profiling of spreading-coupled protein tyrosine phosphorylation in migratory cells

Xie

Wang

Zhang

et al. 2016

Sci Rep

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Protein tyrosine phosphorylation is an important mechanism that regulates cytoskeleton reorganization and cell spreading of migratory cells. A number of cytoskeletal proteins are known to be tyrosine phosphorylated (pY) in different cellular processes. However, the profile of pY proteins during different stages of cell spreading has not been available. Using immunoafffinity enrichment of pY proteins coupled with label free quantitative proteomics, we quantitatively identified 447 pY proteins in the migratory ECV-304 cells at the early spreading (adhesion) and the active spreading stages. We found that pY levels of the majority of the quantified proteins were significantly increased in the active spreading stage compared with the early spreading stage, suggesting that active cell spreading is concomitant with extra tyrosine phosphorylation. The major categories of proteins impacted by tyrosine phosphorylation are involved in cytoskeleton and focal adhesion regulation, protein translation and degradation. Our findings, for the first time, dissect the cell spreading-specific pY signals from the adhesion induced pY signals, and provide a valuable resource for the future mechanistic research regarding the regulation of cell spreading.

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Section: Discussionsupporting

confidence: 61%

Quantitative profiling of spreading-coupled protein tyrosine phosphorylation in migratory cells

Xie

Wang

Zhang

et al. 2016

Sci Rep

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“…Initial candidate-based proteomic studies of integrins and IAC components identified post-translational modifications and/or interacting partners (Humphries et al, 2015); however, a step change came with the development of methods to isolate integrin-containing ventral membrane preparations. These methods relied on stabilisation of IACs using chemical cross-linkers and enrichment of IAC components by removal of the cell body and cytoplasmic proteins (Jones et al, 2015; Kuo et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

The integrin adhesome network at a glance

Horton

Humphries

James

et al. 2016

Journal of Cell Science

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187

132

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The adhesion nexus is the site at which integrin receptors bridge intracellular cytoskeletal and extracellular matrix networks. The connection between integrins and the cytoskeleton is mediated by a dynamic integrin adhesion complex (IAC), the components of which transduce chemical and mechanical signals to control a multitude of cellular functions. In this Cell Science at a Glance article and the accompanying poster, we integrate the consensus adhesome, a set of 60 proteins that have been most commonly identified in isolated IAC proteomes, with the literature-curated adhesome, a theoretical network that has been assembled through scholarly analysis of proteins that localise to IACs. The resulting IAC network, which comprises four broad signalling and actin-bridging axes, provides a platform for future studies of the regulation and function of the adhesion nexus in health and disease.

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“…Integrins recruit adaptor and signaling proteins to macromolecular complexes called FAs that connect to the actin cytoskeleton [15–17]. Proteomic techniques have identified hundreds of adaptor and signaling proteins that differentially and dynamically target to integrin adhesions [18], while nanoscopic imaging has begun to reveal their three-dimension organization within cells [19].…”

Section: Integrin Adhesion Complex Components Dynamics and Functionmentioning

confidence: 99%

“…For example, vinculin is one key protein that has multiple FA functions from regulation of maturation to ECM mechanosensing [24, 25], and has over 14 binding partners, which differentially target to all three nanodomains. Extensive research has shown that FAs serve numerous and diverse functions within cells [17]. One of the best understood roles of FAs is the regulation of cell migration on ECM proteins by allowing dynamic linkages with anchored integrin receptors [26].…”

Section: Integrin Adhesion Complex Components Dynamics and Functionmentioning

confidence: 99%

Cell adhesion and invasion mechanisms that guide developing axons

Short

Suarez-Zayas

Gómez

2016

Current Opinion in Neurobiology

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Axon extension, guidance and tissue invasion share many similarities to normal cell migration and cancer cell metastasis. Proper cell and growth cone migration requires tightly regulated adhesion complex assembly and detachment from the extracellular matrix (ECM). In addition, many cell types actively remodel the ECM using matrix metalloproteases (MMPs) to control tissue invasion and cell dispersal. Targeting and activating MMPs is a tightly regulated process, that when dysregulated, can lead to cancer cell metastasis. Interestingly, new evidence suggests that growth cones express similar cellular and molecular machinery as migrating cells to clutch retrograde actin flow on ECM proteins and target matrix degradation, which may be used to facilitate axon pathfinding through the basal lamina and across tissues.

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Emerging properties of adhesion complexes: what are they and what do they do?

Cited by 76 publications

References 123 publications

Quantitative profiling of spreading-coupled protein tyrosine phosphorylation in migratory cells

Quantitative profiling of spreading-coupled protein tyrosine phosphorylation in migratory cells

The integrin adhesome network at a glance

Cell adhesion and invasion mechanisms that guide developing axons

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