Semaphorin 7a Promotes Spreading and Dendricity in Human Melanocytes through β1-Integrins

Scott, Glynis; McClelland, Lindy; Fricke, Alex F.

doi:10.1038/sj.jid.5700974

Cited by 75 publications

(94 citation statements)

References 57 publications

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“…In fact, SEMA7A promotes cell spreading and dendricity (in melanocytes) via β1 integrin (Scott et al, 2008a), whereas it can inhibit cell-substrate adhesion (in dendritic cells) by binding to plexin-C1 (Walzer et al, 2005). Cofilin, an actinbinding protein that is implicated in cell migration, seems to be a common mediator, which is regulated in an opposing manner on activation of the two different receptors by SEMA7A (Scott et al, 2008b).…”

Section: Examples Of Cell-type-specific Effects Of Semaphorinsmentioning

confidence: 99%

Semaphorin signaling in cancer cells and in cells of the tumor microenvironment – two sides of a coin

Capparuccia

Tamagnone

2009

Journal of Cell Science

173

154

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Journal of Cell Science 1724 including cell-adhesion molecule L1 (Castellani and Rougon, 2002) and the receptor tyrosine kinases (RTKs) VEGFR2 (Toyofuku et al., 2004), erythroblastic leukemia viral oncogene homolog 2 (ErbB2) (Swiercz et al., 2004), off-track kinase (OTK) (Winberg et al., 2001) and Met (also known as HGFR) (Giordano et al., 2002). In the immune system, CD72 and Tim2 (T-cell immunoglobulin and mucin domain-containing protein 2) were found to interact functionally (although with low affinity) with the transmembrane semaphorins SEMA4D and SEMA4A, respectively (Kumanogoh et al., 2002;Kumanogoh et al., 2000). Recently, other ligands for NPs have also been described, including fibroblast growth factor 2 (FGF2) (West et al., 2005), hepatocyte growth factor (HGF) (Sulpice et al., 2008) and galectin-1 (Gal-1) (Hsieh et al., 2008). In addition, NPs were recently observed to form complexes with additional cell-surface receptors, including Met (Matsushita et al., 2007), β1 integrin (Fukasawa et al., 2007) and transforming growth factor-β1 (TGF-β1) (Glinka and Prud'homme, 2008) (for reviews see Neufeld and Kessler, 2008;Pellet-Many et al., 2008).In addition to their function in a range of basic cellular processes, recent studies have shown that semaphorin-mediated signals might also play important regulatory functions in cancer . On one side, tumor progression and metastatic dissemination depend on intrinsic properties of cancer cells, such as survival, self-renewal and the ability to migrate and overcome tissue barriers (invasiveness). On the other side, the tumor stroma -which includes endothelial cells, fibroblasts and cells of the immune system -is engaged in active molecular crosstalk with cancer cells. For example, blood-and lymph-vessel angiogenesis, together with inflammatory and immunosuppressive responses, further promotes cancer-cell survival, migration and invasion, as well as initiation of the metastatic cascade. In this Commentary, we review the current knowledge on the emerging role of semaphorin signals in controlling these 'two sides of a coin' -that is, the tumor-cell intrinsic alterations, and the crosstalk between cancer cells and other cells of the tumor microenvironment. In addition, the implications of semaphorin signaling in tumor progression will be discussed. . Of the vertebrate semaphorins, those in classes 4, 5 and 6 are transmembrane proteins, whereas those in class 7 are membrane-anchored via glycophosphatidylinositol (GPI). Class-3 secreted semaphorins have C-terminal basic-charged sequences, which are required for binding to neuropilins. Several class-3 semaphorins and SEMA4D have been shown to undergo regulatory cleavage by furins or metalloproteases. Class-5 semaphorins are distinguished by thrombospondin repeats. Several semaphorins also contain immunoglobulin-like domains. (B) Neuropilins are transmembrane receptors that are characterized by two complement-like (CUB) domains (also called the a1 and a2 domains), two FV/FVIII coagulation factor-like domains (also called the...

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Section: Examples Of Cell-type-specific Effects Of Semaphorinsmentioning

confidence: 99%

Semaphorin signaling in cancer cells and in cells of the tumor microenvironment – two sides of a coin

Capparuccia

Tamagnone

2009

Journal of Cell Science

173

154

View full text Add to dashboard Cite

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“…The pleiotropic nature of semaphorins is particularly evident for Sema7A, whose roles in immune function [74] and cancer biology [75,76,77] have been extensively studied. In addition, a few reports have addressed its role in neuronal development [78,79,80,81,82].…”

Section: Semaphorin Expression and Role In The Development Of The Olfmentioning

confidence: 99%

Shaping the Reproductive System: Role of Semaphorins in Gonadotropin-Releasing Hormone Development and Function

Giacobini¹

2015

Neuroendocrinology

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The semaphorin proteins, which contribute to the morphogenesis and homeostasis of a wide range of systems, are among the best-studied families of guidance cues. Much recent research has focused on the role of semaphorins in the development and adult activity of hormone systems and, reciprocally, how circulating reproductive hormones regulate their expression and function. Specifically, several reports have focused on the molecular mechanisms underlying the effects of semaphorins on the migration, survival and structural and functional plasticity of neurons that secrete gonadotropin-releasing hormone (GnRH), essential for the acquisition and maintenance of reproductive competence in mammals. Alterations in the development of this neuroendocrine system lead to anomalous or absent GnRH secretion, resulting in heterogeneous reproductive disorders such as congenital hypogonadotropic hypogonadism (CHH) or other conditions characterized by infertility or subfertility. This review summarizes current knowledge of the role of semaphorins and their receptors on the development, differentiation and plasticity of the GnRH system. In addition, the involvement of genetic deficits in semaphorin signaling in some forms of CHH in humans is discussed.

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“…Thus, Sema7A on DCs acts by controlling the balance between adhesion/ deadhesion, similar to Sema7A function on tumor cells and melanocytes (15,17,38). A prominent role for the actin-binding protein cofilin was shown in these studies.…”

Section: Discussionmentioning

confidence: 71%

“…Because Sema7A was demonstrated to regulate cell adhesion/ migration in the neuronal system and in skin tumors (16,17), we hypothesized that Sema7A on DCs may be involved in the regulation of adhesion and/or migration during DC maturation.…”

Section: Sema7a Modulates DC Migration In Vivomentioning

confidence: 99%

“…Binding of Sema7A to plexin C1 in melanocytes leads to inhibition of the actin-binding protein cofilin and reduced cell spreading (15). In contrast, Sema7A binding to integrins in neurons or melanocytes activates FAK and MAPK pathways, leading to remodeling of the actin cytoskeleton and increased cell spreading (16,17). Thus, Sema7A regulates two signaling pathways that have counteracting effects on the actin cytoskeleton and cell adhesion.…”

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Semaphorin 7A Promotes Chemokine-Driven Dendritic Cell Migration

Rijn

Paulis

Riet

et al. 2016

The Journal of Immunology

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Dendritic cell (DC) migration is essential for efficient host defense against pathogens and cancer, as well as for the efficacy of DC-based immunotherapies. However, the molecules that induce the migratory phenotype of DCs are poorly defined. Based on a large-scale proteome analysis of maturing DCs, we identified the GPI-anchored protein semaphorin 7A (Sema7A) as being highly expressed on activated primary myeloid and plasmacytoid DCs in human and mouse. We demonstrate that Sema7A deficiency results in impaired chemokine CCL21-driven DC migration in vivo. Impaired formation of actin-based protrusions, resulting in slower three-dimensional migration, was identified as the mechanism underlying the DC migration defect. Furthermore, we show, by atomic force microscopy, that Sema7A decreases adhesion strength to extracellular matrix while increasing the connectivity of adhesion receptors to the actin cytoskeleton. This study demonstrates that Sema7A controls the assembly of actin-based protrusions that drive DC migration in response to CCL21.

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Semaphorin 7a Promotes Spreading and Dendricity in Human Melanocytes through β1-Integrins

Cited by 75 publications

References 57 publications

Semaphorin signaling in cancer cells and in cells of the tumor microenvironment – two sides of a coin

Semaphorin signaling in cancer cells and in cells of the tumor microenvironment – two sides of a coin

Shaping the Reproductive System: Role of Semaphorins in Gonadotropin-Releasing Hormone Development and Function

Semaphorin 7A Promotes Chemokine-Driven Dendritic Cell Migration

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