Neuronal pentraxin with chromo domain (NPCD) is a novel class of protein expressed in multiple neuronal domains

Chen, Bin; Bixby, John L.

doi:10.1002/cne.20391

Cited by 19 publications

(27 citation statements)

References 23 publications

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“…We screened 4 ϫ 10 6 cDNA clones and identified a total of 53 positive clones. Of these, 27 were strongly interacting clones as assessed by intense blue color (MEL1); all 27 represented a 1.1 kb partial cDNA clone of the neuronal pentraxin receptor (Dodds et al, 1997;Chen and Bixby, 2005).…”

Section: Resultsmentioning

confidence: 99%

“…Although this argues against a relevant interaction between NPR and the intracellular domain of PTPRO, we have discovered recently that NPR is a splice variant of the extended NPCD gene, alternative splicing of which produces multiple isoforms encoding intracellular pentraxins fused to an N-terminal chromatin organization modifier (chromo) domain. These NPCD proteins are localized in the cytoplasm and can be associated with the plasma membrane (Chen and Bixby, 2005). The 1.1 kb cDNA from the two-hybrid screen encodes a fragment of NPCD comprising aa 136 -494 of the published sequence.…”

Section: Resultsmentioning

confidence: 99%

“…Affinity-purified antibodies to the chromo domain (anti-CD) and to the pentraxin domain (anti-Ptx) of NPCD have been described (Chen and Bixby, 2005). MAP2 monoclonal antibody and actin monoclonal antibody were from Sigma (St. Louis, MO), GFAP polyclonal antibody was from DakoCytomation (Carpinteria, CA), L1 polyclonal antibody was a generous gift from Dr. Vance Lemmon (University of Miami, Miami, FL), anti-phosphotyrosine (4G10) was from Upstate Biotechnology (Lake Placid, NY), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) monoclonal antibody was from Ambion (Austin, TX).…”

Section: Methodsmentioning

confidence: 99%

“…However, the two-hybrid interaction could be an artifact of the yeast system. To test protein interactions in a mammalian cell system, we coexpressed the PTPRO intracellular domain and the 41 kDa NPCD protein (Chen and Bixby, 2005) in COS cells. Immunoprecipitation of PTPRO brought down NPCD, and immunoprecipitation of NPCD brought down PTPRO (supplementary Fig.…”

Section: Npcd Interacts With Ptpro In Mammalian Cellsmentioning

confidence: 99%

“…In this screen, we identified a fragment of the gene previously known as the neuronal pentraxin receptor (NPR), which we have renamed neuronal pentraxin with chromo domain (NPCD). NPCD has a number of different isoforms, formed by alternative splicing, with an unusual motif structure combining a chromatin organizer modifier (chromo) domain and a neuronal pentraxin domain (Chen and Bixby, 2005).…”

Section: Introductionmentioning

confidence: 99%

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A Novel Substrate of Receptor Tyrosine Phosphatase PTPRO Is Required for Nerve Growth Factor-Induced Process Outgrowth

Chen¹,

Bixby²

2005

J. Neurosci.

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The receptor protein tyrosine phosphatase PTPRO may be involved in axon guidance both as a ligand and as a neuronal receptor. We have begun to characterize signaling by PTPRO as a receptor by screening for proteins interacting with the intracellular domain of PTPRO. In a yeast-two hybrid screen, we identified a novel class of protein, which we named neuronal pentraxin with chromo domain (NPCD), as a PTPRO-interacting protein. We have shown recently that NPCD has multiple cytoplasmic isoforms as a result of alternative splicing and that these proteins are present in many neurons, mainly associated with the inner side of the plasma membrane. Through additional two-hybrid experiments, cotransfection and reciprocal coprecipitation, glutathione S-transferase pulldown, and immunoprecipitation in vivo, we confirm that NPCD isoforms interact with the catalytic phosphatase domain of PTPRO. We also find that at least one NPCD isoform is tyrosine phosphorylated in vivo and can serve as a substrate for PTPRO in vitro. Analysis of PTPRO knock-out mice demonstrates that normal localization of NPCD at the plasma membrane requires PTPRO expression, suggesting a physiological role for the NPCD/PTPRO interaction. NPCD is likely to be relevant to axon growth and/or guidance, because RNA interference mediated knockdown of NPCD expression in pheochromocytoma cells inhibits NGF-induced neuronal process outgrowth without affecting NGFdependent survival or initial NGF signaling.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Npcd Interacts With Ptpro In Mammalian Cellsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

A Novel Substrate of Receptor Tyrosine Phosphatase PTPRO Is Required for Nerve Growth Factor-Induced Process Outgrowth

Chen¹,

Bixby²

2005

J. Neurosci.

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PPTX, a pentraxin domain‐containing protein, interacts with the T1 domain of K_v4

Harvey

Karolat

Sakai

et al. 2009

J of Neuroscience Research

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Voltage-gated K(+) (K(v)) channels reside as tetramers in the membrane. The events that coordinate folding, trafficking, and tetramerization are mediated by an array of associated proteins and phospholipids whose identification is vital to understanding the dynamic nature of channel expression and activity. An interaction between an A-type K(+) channel, K(v)4.2, and a protein containing a pentraxin domain (PPTX) was demonstrated in the cochlea (Duzhyy et al. [ 2005] J. Biol. Chem. 280:15165-15172). Here, we present results based on fold recognition and homology modeling that revealed the tetramerization (T1) domain of K(v)4.2 as a potential docking site for interacting proteins such as PPTX. By using this model, putative sites were experimentally tested with the yeast two-hybrid system to assay interactions between PPTX and the T1 domain of K(v)4.2 wild type (wt) and mutants (mut). Results showed that amino acid residues 86 and 118 in the T1 domain are essential for interaction, because replacing these negatively charged with neutrally charged amino acids inhibits interactions. Cotransfections of Chinese hamster ovary cells with PPTX and K(v)4.2wt further revealed that PPTX increases K(v)4.2 wt expression in vitro when analyzing total lysates, whereas interactions with K(v)4.2 microt resulted in a decrease. These studies suggest that portions of the T1 domain can act as docking sites for proteins such as PPTX, further underscoring the significance of this domain.

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Protein tyrosine phosphatase receptor type O (Ptpro) regulates cerebellar formation during zebrafish development through modulating Fgf signaling

Liao

Cheng

Hung

et al. 2013

Cell. Mol. Life Sci.

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Protein activities controlled by receptor protein tyrosine phosphatases (RPTPs) play comparably important roles in transducing cell surface signals into the cytoplasm by protein tyrosine kinases. Previous studies showed that several RPTPs are involved in neuronal generation, migration, and axon guidance in Drosophila, and the vertebrate hippocampus, retina, and developing limbs. However, whether the protein tyrosine phosphatase type O (ptpro), one kind of RPTP, participates in regulating vertebrate brain development is largely unknown. We isolated the zebrafish ptpro gene and found that its transcripts are primarily expressed in the embryonic and adult central nervous system. Depletion of zebrafish embryonic Ptpro by antisense morpholino oligonucleotide knockdown resulted in prominent defects in the forebrain and cerebellum, and the injected larvae died on the 4th day post-fertilization (dpf). We further investigated the function of ptpro in cerebellar development and found that the expression of ephrin-A5b (efnA5b), a Fgf signaling induced cerebellum patterning factor, was decreased while the expression of dusp6, a negative-feedback gene of Fgf signaling in the midbrain-hindbrain boundary region, was notably induced in ptpro morphants. Further analyses demonstrated that cerebellar defects of ptpro morphants were partially rescued by inhibiting Fgf signaling. Moreover, Ptpro physically interacted with the Fgf receptor 1a (Fgfr1a) and dephosphorylated Fgfr1a in a dose-dependant manner. Therefore, our findings demonstrate that Ptpro activity is required for patterning the zebrafish embryonic brain. Specifically, Ptpro regulates cerebellar formation during zebrafish development through modulating Fgf signaling.Electronic supplementary materialThe online version of this article (doi:10.1007/s00018-013-1259-7) contains supplementary material, which is available to authorized users.

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Neuronal pentraxin with chromo domain (NPCD) is a novel class of protein expressed in multiple neuronal domains

Cited by 19 publications

References 23 publications

A Novel Substrate of Receptor Tyrosine Phosphatase PTPRO Is Required for Nerve Growth Factor-Induced Process Outgrowth

A Novel Substrate of Receptor Tyrosine Phosphatase PTPRO Is Required for Nerve Growth Factor-Induced Process Outgrowth

PPTX, a pentraxin domain‐containing protein, interacts with the T1 domain of K_v4

Protein tyrosine phosphatase receptor type O (Ptpro) regulates cerebellar formation during zebrafish development through modulating Fgf signaling

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Neuronal pentraxin with chromo domain (NPCD) is a novel class of protein expressed in multiple neuronal domains

Cited by 19 publications

References 23 publications

A Novel Substrate of Receptor Tyrosine Phosphatase PTPRO Is Required for Nerve Growth Factor-Induced Process Outgrowth

A Novel Substrate of Receptor Tyrosine Phosphatase PTPRO Is Required for Nerve Growth Factor-Induced Process Outgrowth

PPTX, a pentraxin domain‐containing protein, interacts with the T1 domain of Kv4

Protein tyrosine phosphatase receptor type O (Ptpro) regulates cerebellar formation during zebrafish development through modulating Fgf signaling

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PPTX, a pentraxin domain‐containing protein, interacts with the T1 domain of K_v4