BIG-1: A new TAG-1/F3-related member of the immunoglobulin superfamily with neurite outgrowth-promoting activity

Yoshihara, Yoshihiro; Kawasaki, Mikio; Tani, Akiko; Tamada, Atsushi; Nagata, Shinji; Kagamiyama, Hiroyuki; Mori, Kensaku

doi:10.1016/0896-6273(94)90357-3

Cited by 97 publications

(74 citation statements)

References 47 publications

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“…The data presented here in addition to the expression pattern of PTPRG suggest that PTPRG could be the CNTN4-binding protein found in the olfactory bulb. Although less is known about the function of CNTN3, its expression in the olfactory bulb of adult mice matches the expression pattern of PTPRG indicating that a physical interaction is possible in vivo (4,23).…”

Section: Discussionmentioning

confidence: 96%

The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members of the contactin family of neural recognition molecules

Bouyain

Watkins

2010

Proc. Natl. Acad. Sci. U.S.A.

105

128

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The receptor protein tyrosine phosphatases gamma (PTPRG) and zeta (PTPRZ) are expressed primarily in the nervous system and mediate cell adhesion and signaling events during development. We report here the crystal structures of the carbonic anhydrase-like domains of PTPRZ and PTPRG and show that these domains interact directly with the second and third immunoglobulin repeats of the members of the contactin (CNTN) family of neural recognition molecules. Interestingly, these receptors exhibit distinct specificities: PTPRZ binds only to CNTN1, whereas PTPRG interacts with CNTN3, 4, 5, and 6. Furthermore, we present crystal structures of the four N-terminal immunoglobulin repeats of mouse CNTN4 both alone and in complex with the carbonic anhydrase-like domain of mouse PTPRG. In these structures, the N-terminal region of CNTN4 adopts a horseshoe-like conformation found also in CNTN2 and most likely in all CNTNs. This restrained conformation of the second and third immunoglobulin domains creates a binding site that is conserved among CNTN3, 4, 5, and 6. This site contacts a discrete region of PTPRG composed primarily of an extended β-hairpin loop found in both PTPRG and PTPRZ. Overall, these findings implicate PTPRG, PTPRZ and CNTNs as a group of receptors and ligands involved in the manifold recognition events that underlie the construction of neural networks.cell adhesion | crystal structure | Ig superfamily | receptor protein tyrosine phosphatase

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Section: Discussionmentioning

confidence: 96%

The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members of the contactin family of neural recognition molecules

Bouyain

Watkins

2010

Proc. Natl. Acad. Sci. U.S.A.

105

128

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“…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. Some of the GPIlinked IgSF proteins are involved in a variety of specific cell-cell interactions and/or in migration, such as LAMP, BIG-1, neurotrimin, CEPU-1, GP55 [7][8][9], CEA, CEACAM-6, NCAM p120 [10][11][12], F3/F11/contactin and TAG1/axonin-1 [13,14]. In addition, the presence of the MAM and/or Ig domains confers to these proteins the capacity to interact with other cells through homophilic and/or heterophilic interactions [2,4,15].…”

Section: Introductionmentioning

confidence: 99%

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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“…membrane anchorage and particular combinations of Ig and FNIII domains, the family of Ig/ FNIII neural glycoproteins can be divided further into several subgroups (Vielmetter et al, 1994). The glycosylphosphatidylinositol (GPI)-anchored proteins contactin/ F 11/F3, TAG-1/axonin-1, PANG/BIG-I and BIG-2 constitute one such subgroup and are striking particularly in their spatially and temporally restricted patterns of expression during neuronal development (Ranscht, 1988;Brummendorf et al, 1989;Gennarini et al, 1989;Furley et al, 1990;Zuellig et al, 1992;Connelly et al, 1994;Yoshihara et al, 1994Yoshihara et al, , 1995. They are composed of six Ig and four FNIII domains separated by a glycine/prolinerich segment.…”

Section: Introductionmentioning

confidence: 99%

Implications for the domain arrangement of axonin-1 derived from the mapping of its NgCAM binding site.

et al. 1996

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Tittmann, P; Gross, H; Sonderegger, P. Implications for the domain arrangement of axonin-1 derived from the mapping of its NgCAM binding site. EMBO J. 1996EMBO J. , 15(9):2056. Postprint available at: http://www.zora.unizh.ch Posted at the Zurich Open Repository and Archive, University of Zurich. http://www.zora.unizh.ch Originally published at: EMBO J. 1996EMBO J. , 15(9):2056 Implications for the domain arrangement of axonin-1 derived from the mapping of its NgCAM binding site AbstractThe neuronal cell adhesion molecule axonin-1 is composed of six immunoglobulin and four fibronectin type III domains. Axonin-1 promotes neurite outgrowth, when presented as a substratum for neurons in vitro, via a neuronal receptor that has been identified as the neuron-glia cell adhesion molecule, NgCAM, based on the blocking effect of polyclonal antibodies directed to NgCAM. Here we report the identification of axonin-1 domains involved in NgCAM binding. NgCAM-conjugated microspheres were tested for binding to COS cells expressing domain deletion mutants of axonin-1. In addition, monoclonal antibodies directed to axonin-1 were assessed for their ability to block the axonin-1-NgCAM interaction, and their epitopes were mapped using the domain deletion mutants. The results suggest that the four amino-terminal immunoglobulin domains of axonin-1 form a domain conglomerate which is necessary and sufficient for NgCAM binding. Surprisingly, NgCAM binding to membrane-bound axonin-1 was increased strongly by deletion of the fifth or sixth immunoglobulin domains of axonin-1. Based on these results and on negative staining electron microscopy, we propose a horseshoe-shaped domain arrangement of axonin-1 that obscures the NgCAM binding site. Neurite outgrowth studies with truncated forms of axonin-1 show that axonin-1 is a neurite outgrowth-promoting substratum in the absence of the NgCAM binding site.The EMBO Journal vol.15 no.9 pp.2056-2068, 1996 Implications for the domain arrangement of axonin-1 derived from the mapping of

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BIG-1: A new TAG-1/F3-related member of the immunoglobulin superfamily with neurite outgrowth-promoting activity

Cited by 97 publications

References 47 publications

The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members of the contactin family of neural recognition molecules

The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members of the contactin family of neural recognition molecules

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

Implications for the domain arrangement of axonin-1 derived from the mapping of its NgCAM binding site.

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