Receptor protein tyrosine phosphatases are expressed by cycling retinal progenitor cells and involved in neuronal development of mouse retina

Horvat-Bröcker, Andrea; Reinhard, Jacqueline; Illes, Sebastian; Paech, T.; Zoidl, Georg; Harroch, Sheila; Distler, C.; Knyazev, Piotr; Ullrich, Axel; Faissner, Andréas

doi:10.1016/j.neuroscience.2008.01.016

Cited by 21 publications

(21 citation statements)

References 107 publications

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“…S3, A and B). Consistent with previous findings (16), a strong signal could be observed for PTPRG in the OSs, ISs, inner plexiform layer, and GCL. By contrast, CNTN3 was mostly localized to the OS, where it overlapped with PTPRG ( Fig.…”

Section: Identification Of a Ptprg⅐cntn Complex In Adult Mousesupporting

confidence: 92%

“…5) (16). Notably, Ptprg null mice do not exhibit any morphological defect in retinas, suggesting that PTPRG is not necessary for retinal development (16). However, previous studies have shown that rod cyclic nucleotide-gated (CNG) channels in the outer segments can be modulated by phosphorylation of a specific tyrosine residue (Tyr 498 ) located in the cyclic nucleotide-binding domain of the ␣-subunit of the channel protein (37,38).…”

Section: Discussionmentioning

confidence: 99%

“…This question was addressed in mouse retinas, where PTPRG and CNTN3-5 are expressed (10,16). In simple terms, the retina includes three major neuronal layers (Fig.…”

Section: Identification Of a Ptprg⅐cntn Complex In Adult Mousementioning

confidence: 99%

“…Less is known, however, about the physiological function of CNTN3, although cntn3 transcripts have been detected in the granule cell layers of the olfactory bulb and Purkinje cells of the cerebellum (15). In broad terms, the sites and times of CNTN3-6 expression match those of PTPRG expression in sensory neurons, such as retinal ganglion cells, the cells of the glomerulus in the olfactory bulb, and ear sensory cells (4,16). However, the formation of complexes between PTPRG and CNTN3-6 has yet to be confirmed in vivo.…”

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confidence: 99%

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Structural Basis for Interactions Between Contactin Family Members and Protein-tyrosine Phosphatase Receptor Type G in Neural Tissues

Nikolaienko

Hammel

Dubreuil

et al. 2016

Journal of Biological Chemistry

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Protein-tyrosine phosphatase receptor type G (RPTP␥/ PTPRG) interacts in vitro with contactin-3-6 (CNTN3-6), a group of glycophosphatidylinositol-anchored cell adhesion molecules involved in the wiring of the nervous system. In addition to PTPRG, CNTNs associate with multiple transmembrane proteins and signal inside the cell via cis-binding partners to alleviate the absence of an intracellular region. Here, we use comprehensive biochemical and structural analyses to demonstrate that PTPRG⅐CNTN3-6 complexes share similar binding affinities and a conserved arrangement. Furthermore, as a first step to identifying PTPRG⅐CNTN complexes in vivo, we found that PTPRG and CNTN3 associate in the outer segments of mouse rod photoreceptor cells. In particular, PTPRG and CNTN3 form cis-complexes at the surface of photoreceptors yet interact in trans when expressed on the surfaces of apposing cells. Further structural analyses suggest that all CNTN ectodomains adopt a bent conformation and might lie parallel to the cell surface to accommodate these cis and trans binding modes. Taken together, these studies identify a PTPRG⅐CNTN complex in vivo and provide novel insights into PTPRG-and CNTN-mediated signaling.The complex processes that shape the nervous system include the proliferation, differentiation, and migration of neural cells, axon guidance, and the formation of synapses. At the molecular level, these intricate processes rely on interactions between cell surface receptors coupled to intracellular downstream signaling networks. Such receptors might include cadherins, Ig superfamily proteins, neurexins, neuroligins, and leucine-rich repeat proteins as well as receptor tyrosine kinases and receptor protein-tyrosine phosphatases (RPTPs) 4 (1, 2). Members of the RPTP family typically combine large extracellular segments and intracellular phosphatase domains, which makes them ideally suited to coordinate cell adhesion and cell signaling. Among these, the homologous protein-tyrosine phosphatase receptor type G (PTPRG) and protein-tyrosine phosphatase receptor type Z (PTPRZ) were among the first RPTPs identified in the nervous system, and their ectodomains are characterized by the presence of an inactive N-terminal carbonic anhydrase-like (CA) domain that mediates proteinprotein interactions (Fig. 1A) (3, 4). PTPRZ and its binding partner, the neural cell adhesion molecule contactin-1 (CNTN1), control the proliferation of oligodendrocyte precursor cells and their maturation into myelinating oligodendrocytes (5). Less is known, however, about PTPRG, its in vivo ligands, and the physiological roles these complexes might play.Unlike PTPRZ, PTPRG is mostly expressed on neurons, although it has recently been found in some astrocytes and microglia in adult mouse brains (4, 6). PTPRG interacts in vitro via its CA domain with four homologs of CNTN1 called CNTN3-6 (7). All CNTNs are linked to the membrane by a glycophosphatidylinositol (GPI) anchor, suggesting that they require a co-receptor to signal across the membrane (8, 9). CNTNs a...

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Section: Identification Of a Ptprg⅐cntn Complex In Adult Mousesupporting

confidence: 92%

Section: Discussionmentioning

confidence: 99%

“…This question was addressed in mouse retinas, where PTPRG and CNTN3-5 are expressed (10,16). In simple terms, the retina includes three major neuronal layers (Fig.…”

Section: Identification Of a Ptprg⅐cntn Complex In Adult Mousementioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Structural Basis for Interactions Between Contactin Family Members and Protein-tyrosine Phosphatase Receptor Type G in Neural Tissues

Nikolaienko

Hammel

Dubreuil

et al. 2016

Journal of Biological Chemistry

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“…In a first step, the expression of the Tnc interaction partners Phosphacan and RPTPb/z-long was investigated. These proteins also occur as chondroitin sulfate proteoglycans (CSPGs) that bear a specific carbohydrate motif recognized by the monoclonal antibody 473HD (Barnea et al, 1994;Grumet et al, 1994;Klausmeyer et al, 2007) and is expressed by radial glia neural stem/progenitor cells (Horvat-Brocker et al, 2008;von Holst et al, 2006). Immunohistochemical stainings, the quantification of immunopositive single cells and Western blotting evidenced an up-regulation of this CS-epitope in the Tnc-deficient tissue.…”

Section: Discussionmentioning

confidence: 99%

Tenascin C regulates proliferation and differentiation processes during embryonic retinogenesis and modulates the de-differentiation capacity of Müller glia by influencing growth factor responsiveness and the extracellular matrix compartment

Besser

Jagatheaswaran

Reinhard

et al. 2012

Developmental Biology

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The retina represents an ideal model system for studying developmental processes during morphogenesis. The knowledge of the precise regulation and combination of genetic pre-dispositions and environmental circumstances enables the understanding of pathologies and the subsequent development or/and improvement of therapeutic strategies. This study focused on the functional analysis of the extracellular matrix (ECM) molecule Tenascin C (Tnc) in the retinal stem/progenitor cell environment. In this perspective, a Tnc(-/-) mouse was examined for potential alterations in proliferation and differentiation programs by using immunohistochemistry, RT-PCR analysis and bioassays. It could be shown that both cycling G2-phase cells and early post-mitotic neurons were significantly increased in the retina due to Tnc-deficiency. Further investigations suggested that Tnc regulates these processes via the Wnt-signaling cascade. Therapeutic approaches in the treatment of degenerative diseases often integrate cell-replacement strategies. Retinal Müller glia cells represent the glia of the retina and are described to possess the ability to re-enter the cell cycle and generate neurons in response to injury. In this study, the de-differentiation was induced by FGF2. It was found out that Tnc influences the de-differentiation behavior of adherent Müller glia in vitro. Moreover, it was interesting to investigate the effect of the absence of Tnc on the composition of other components of the ECM. A special focus lay on the expression of a specifically sulfated carbohydrate motif on chondroitin sulfate glycosaminoglycan chains, which can be detected with the mAb 473HD. It was possible to note a significant increase of this particular chondroitin sulfate in the Tnc-deficient ECM.

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Retinal Anatomy of the New Zealand Kiwi: Structural Traits Consistent With Their Nocturnal Behavior

Corfield

Parsons

Harimoto

et al. 2014

The Anatomical Record

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Kiwi (Apteryx spp.) have a visual system unlike that of other nocturnal birds, and have specializations to their auditory, olfactory, and tactile systems. Eye size, binocular visual fields and visual brain centers in kiwi are proportionally the smallest yet recorded among birds. Given the many unique features of the kiwi visual system, we examined the laminar organization of the kiwi retina to determine if they evolved increased light sensitivity with a shift to a nocturnal niche or if they retained features of their diurnal ancestor. The laminar organization of the kiwi retina was consistent with an ability to detect low light levels similar to that of other nocturnal species. In particular, the retina appeared to have a high proportion of rod photoreceptors as compared to diurnal species, as evidenced by a thick outer nuclear layer, and also numerous thin photoreceptor segments intercalated among the conical shaped cone photoreceptor inner segments. Therefore, the retinal structure of kiwi was consistent with increased light sensitivity, although other features of the visual system, such as eye size, suggest a reduced reliance on vision. The unique combination of a nocturnal retina and smaller than expected eye size, binocular visual fields, and brain regions make the kiwi visual system unlike that of any bird examined to date. Whether these features of their visual system are an evolutionary design that meets their specific visual needs or are a remnant of a kiwi ancestor that relied more heavily on vision is yet to be determined. Anat Rec, 298:771-779, 2015. V C 2014 Wiley Periodicals, Inc.

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Receptor protein tyrosine phosphatases are expressed by cycling retinal progenitor cells and involved in neuronal development of mouse retina

Cited by 21 publications

References 107 publications

Structural Basis for Interactions Between Contactin Family Members and Protein-tyrosine Phosphatase Receptor Type G in Neural Tissues

Structural Basis for Interactions Between Contactin Family Members and Protein-tyrosine Phosphatase Receptor Type G in Neural Tissues

Tenascin C regulates proliferation and differentiation processes during embryonic retinogenesis and modulates the de-differentiation capacity of Müller glia by influencing growth factor responsiveness and the extracellular matrix compartment

Retinal Anatomy of the New Zealand Kiwi: Structural Traits Consistent With Their Nocturnal Behavior

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