The integrin—growth factor receptor duet

Alam, Naved; Goel, Hira Lal; Zarif, Matthew J.; Butterfield, Julie Elyssa; Perkins, Hillary M.; Sansoucy, Brian; Sawyer, Thomas K.; Languino, Lucia R.

doi:10.1002/jcp.21278

Cited by 155 publications

(129 citation statements)

References 61 publications

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“…Based on extensive searches of the human and mouse genomic sequences, 18a-and 8b-subunits are known to assemble into 24 integrins. 1,2) Among these integrins, 12 members containing b1 subunit have been found (Fig. 1B).…”

Section: Introductionmentioning

confidence: 96%

Importance of N-Glycosylation on .ALPHA.5.BETA.1 Integrin for Its Biological Functions

Isaji

Sato

et al. 2009

Biological & Pharmaceutical Bulletin

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N-Glycosylation of proteins is conserved in eukaryotes, which is one of the most abundant post-translational modification reactions, and nearly half of all known proteins in eukaryotes are glycosylated. In fact, changes in oligosaccharide structure (glycan) are associated with many physiological and pathological events, including cell adhesion, migration, cell growth, cell differentiation and tumor invasion. Glycosylation reactions are catalyzed by the action of glycosyltransferases, which add sugar chains to various glycans on glycoproteins, glycolipids and proteoglycans. Here, we focus mainly on the modification of N-glycans with N-acetylglucosaminyltransferase III (GnT-III), N-acetylglucosaminyltransferase V (GnT-V) and a a2,6 sialyltransferase (ST6GalI) to address the important roles of N-glycans in integrin-meditaed cell adhesion and migration. In addition, we also discuss the potential roles of N-glycosylation sites on integrin a a5 subunit.

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Section: Introductionmentioning

confidence: 96%

Importance of N-Glycosylation on .ALPHA.5.BETA.1 Integrin for Its Biological Functions

Isaji

Sato

et al. 2009

Biological & Pharmaceutical Bulletin

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“…Integrins can activate several signalling pathways independently (Assoian & Schwartz 2001), but more frequently they act synergistically with other growth factor receptors (Alam et al 2007). Such examples include insulin receptor (Schneller et al 1997 (Schneller et al 1997) and EGF receptor (Bill et al 2004).…”

Section: Integrin and Growth Factor Receptor Signallingmentioning

confidence: 99%

“…The functional activities of these growth factor receptors are dynamically and reciprocally controlled by integrins. The fact that growth factor signalling requires the presence of specific integrin subunits and that different cell types express different profiles of integrins may constitute the 'cellular context' determining the outcome of the growth factor signal (Alam et al 2007). …”

Section: Integrin and Growth Factor Receptor Signallingmentioning

confidence: 99%

“…Integrins are heterodimeric transmembrane receptors composed of eighteen a subunits and eight b subunits that can be non-covalently assembled into 24 combinations. The integrin dimers bind to an array of different ECM molecules with overlapping binding affinities, as summarised in a review by Alam et al (2007). Therefore, the specific integrin expression patterns by a cell dictate which ECM substrate the cell can bind (Hemler & Lobb 1995) and the composition of integrin adhesomes determines the downstream signalling events, thus the eventual cell behaviour and fate.…”

mentioning

confidence: 99%

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Extracellular matrix and cell signalling: the dynamic cooperation of integrin, proteoglycan and growth factor receptor

Kim

Turnbull²,

Guimond³

2011

Journal of Endocrinology

1,004

816

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Extracellular matrices (ECM) are secreted molecules that constitute the cell microenvironment, composed of a dynamic and complex array of glycoproteins, collagens, glycosaminoglycans and proteoglycans. ECM provides the bulk, shape and strength of many tissues in vivo, such as basement membrane, bone and cartilage. In vitro, most animal cells can only grow when they are attached to surfaces through ECM. ECM is also the substrate for cell migration. However, ECM provides much more than just mechanical and structural support, with implications in developmental patterning, stem cell niches and cancer. ECM imparts spatial context for signalling events by various cell surface growth factor receptors and adhesion molecules such as integrins. The external physical properties of ECM may also have a role in the signalling process. ECM molecules can be flexible and extendable, and mechanical tension can expose cryptic sites, which could further interact with growth factors or their receptors. ECM proteins and structures can determine the cell behaviour, polarity, migration, differentiation, proliferation and survival by communicating with the intracellular cytoskeleton and transmission of growth factor signals. Integrins and proteoglycans are the major ECM adhesion receptors which cooperate in signalling events, determining the signalling outcomes, and thus the cell fate. This review focuses on the emerging concept of spatial cell biology of ECM, especially the current understanding of integrins and heparan sulphate proteoglycans as the essential cellular machineries that sense, integrate and respond to the physical and chemical environmental information either by directly connecting with the local adhesion sites or by regulating global cellular processes through growth factor receptor signalling pathways, leading to the integration of both external and internal signals in space and time.

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“…In addition, growth factor receptors and integrins are known to crosstalk (Moro et al, 2002;Yamada and Even-Ram, 2002;Alam et al, 2007;Gilcrease, 2007). Growth factors can be soluble, transmembrane, or ECM bound proteins (Ruoslahti et al, 1992;Massague and Pandiella, 1993;Taipale and Keski-Oja, 1997).…”

Section: Upstream Of Invadopodiamentioning

confidence: 99%

Invadopodia: proteolytic feet of cancer cells

Bati¹,

Pesen-Okvur²

2014

Turk J Biol

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The leading cause of death in cancer patients is metastasis. Invasion is an integral part of metastasis and is carried out by proteolytic structures called invadopodia at the cellular level. In this introductory review, we start by evaluating the definition of invadopodia. While presenting the upstream signaling events involved, we integrate current models on invadopodia. In addition, we discuss the significance of invadopodia in 2D and 3D and in vivo. We finally point out technical challenges and conclude with open questions in the field.

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The integrin—growth factor receptor duet

Cited by 155 publications

References 61 publications

Importance of N-Glycosylation on .ALPHA.5.BETA.1 Integrin for Its Biological Functions

Importance of N-Glycosylation on .ALPHA.5.BETA.1 Integrin for Its Biological Functions

Extracellular matrix and cell signalling: the dynamic cooperation of integrin, proteoglycan and growth factor receptor

Invadopodia: proteolytic feet of cancer cells

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