Characterization of MDGA1, a novel human glycosylphosphatidylinositol-anchored protein localized in lipid rafts

Díaz‐López, Antonio; Rivas, Carmen; Iniesta, Pilar; Morán, Alberto; García-Aranda, Cristina; Megı́as, Diego; Sánchez‐Pernaute, Andrés; Torres, Antonio; Dı́az-Rubio, Eduardo; Benito, Manuel; Juan, Carmen

doi:10.1016/j.yexcr.2005.02.016

Cited by 16 publications

(20 citation statements)

References 34 publications

(33 reference statements)

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“…As observed in its rat (Litwack et al, 2004) and human (Diaz-Lopez et al, 2005) orthologs, chick MDGA1 was a partially secreted, GPI-anchored extracellular molecule (Supplemental figure 1).…”

Section: Fy29/mdga1 Is a Gpi-anchored Extracellular Protein Selectivementioning

confidence: 74%

MDGA1, an IgSF molecule containing a MAM domain, heterophilically associates with axon- and muscle-associated binding partners through distinct structural domains

Fujimura

Iwashita²,

Matsuzaki³

et al. 2006

Brain Research

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Section: Fy29/mdga1 Is a Gpi-anchored Extracellular Protein Selectivementioning

confidence: 74%

MDGA1, an IgSF molecule containing a MAM domain, heterophilically associates with axon- and muscle-associated binding partners through distinct structural domains

Fujimura

Iwashita²,

Matsuzaki³

et al. 2006

Brain Research

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“…We have reported the characterization of the novel human protein MDGA1 (MAM Domain containing Glycosylphosphatidylinositol Anchor-1) [1]. MDGA1 is a 137 kDa protein anchored to the membrane of eukaryotic cells by a GPI motif, which is susceptible to be cleaved by phosphatidylinositolspecific phospholipase C (PI-PLC) [1,2].…”

Section: Introductionmentioning

confidence: 99%

“…MDGA1 is a 137 kDa protein anchored to the membrane of eukaryotic cells by a GPI motif, which is susceptible to be cleaved by phosphatidylinositolspecific phospholipase C (PI-PLC) [1,2]. Similar to other proteins sorted via the secretory pathway, human MDGA1 (hMDGA1) undergoes post-translational modification consisting of N-glycosylation.…”

Section: Introductionmentioning

confidence: 99%

“…Similar to other proteins sorted via the secretory pathway, human MDGA1 (hMDGA1) undergoes post-translational modification consisting of N-glycosylation. Interestingly, hMDGA1 is localized in specialized membrane domains known as lipid rafts [1], providing a hypothetical platform to transduce signals within the cell.…”

Section: Introductionmentioning

confidence: 99%

“…MDGA1 has been postulated as a member of the Ig superfamily (IgSF), the largest class of CAMs, and contains both a MAM domain and a GPI anchor [1][2][3][4][5][6]. The presence of these structural features makes it a unique protein, as it is the first GPI-linked IgSF molecule containing a MAM domain described to our knowledge.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Expression of Human MDGA1 Increases Cell Motility and Cell-Cell Adhesion and Reduces Adhesion to Extracellular Matrix Proteins in MDCK Cells

Díaz‐López

Iniesta

Morán

et al. 2010

Cancer Microenvironment

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Characterization of the novel human protein MDGA1 (MAM Domain containing Glycosylphosphatidylinositol Anchor-1) has been reported in our laboratory in the past few years. hMDGA1 is a glycoprotein containing 955 aminoacids (137 kDa) attached to the eukaryotic cell membrane by a GPI (Glycosylphosphatidylinositol) anchor and localized specifically into membrane microdomains known as lipid rafts. Moreover, MDGA1 protein contains structural features found in different types of cell adhesion molecules (CAMs) such as the presence of immunoglobulin domains and a MAM domain (Meprin, A5 protein, receptor protein-tyrosine phosphatase μ), suggesting a role of MDGA1 in cell migration and/or adhesion. In order to investigate this aim, stable MDCK cell lines expressing MDGA1 or the truncated proteins IgGPI (lacking the MAM domain) and MAMGPI (lacking Ig domains) were generated. Our results reveal that MDGA1 increases the ability of MDCK cells to migrate, as it contains both Ig and MAM domains which have been implicated in cell motility. In addition, cell adhesion to extracellular matrix proteins, mainly to collagen IV, is reduced by MDGA1 and the IgGPI and MAMGPI truncated proteins. Accordingly, silencing MDGA1 by siRNA revealed a significant increase in adhesion to collagen IV. Furthermore, MDGA1 expression, through the intrinsic properties of the MAM domain, increases cell-cell adhesion independently of the cell monolayer used, suggesting that MDGA1 mediates cell-cell adhesiveness in a heterophilic manner.

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Genomewide Association Analysis Followed by a Replication Study Implicates a Novel Candidate Gene for Neuroticism

Oord¹,

Kuo²,

Hartmann³

et al. 2008

Arch Gen Psychiatry

122

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Characterization of MDGA1, a novel human glycosylphosphatidylinositol-anchored protein localized in lipid rafts

Cited by 16 publications

References 34 publications

MDGA1, an IgSF molecule containing a MAM domain, heterophilically associates with axon- and muscle-associated binding partners through distinct structural domains

MDGA1, an IgSF molecule containing a MAM domain, heterophilically associates with axon- and muscle-associated binding partners through distinct structural domains

Expression of Human MDGA1 Increases Cell Motility and Cell-Cell Adhesion and Reduces Adhesion to Extracellular Matrix Proteins in MDCK Cells

Genomewide Association Analysis Followed by a Replication Study Implicates a Novel Candidate Gene for Neuroticism

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