ArticleThe FEBS journal2006
Cell surface nucleolin on developing muscle is a potential ligand for the axonal receptor protein tyrosine phosphatase-sigma.
Article in The FEBS journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 33 citations in OpenAlex.
- Nucleolin mediates the internalization of rabbit hemorrhagic disease virus through clathrin-dependent endocytosis.PLoS pathogens · 2018Article
- Proteomic Analysis of Kveim Reagent Identifies Targets of Cellular Immunity in Sarcoidosis.PloS one · 2017Article
- Cell surface nucleolin facilitates enterovirus 71 binding and infection.Journal of virology · 2015Article
- Cell surface nucleolin interacts with CXCR4 receptor via the 212 c-terminal portion.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015Article
- Nucleolin promotes TGF-β signaling initiation via TGF-β receptor I in glioblastoma.Journal of molecular neuroscience : MN · 2015Article
- Cell surface nucleolin is crucial in the activation of the CXCL12/CXCR4 signaling pathway.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014Article
- Article
- PTPBR7 binding proteins in myelinating neurons of the mouse brain.International journal of biological sciences · 2011Article
- Surface expressed nucleolin is constantly induced in tumor cells to mediate calcium-dependent ligand internalization.PloS one · 2010Article
- Trans-synaptic adhesions between netrin-G ligand-3 (NGL-3) and receptor tyrosine phosphatases LAR, protein-tyrosine phosphatase delta (PTPdelta), and PTPsigma via specific domains regulate excitatory synapse formation.The Journal of biological chemistry · 2010Article
- Article
- Discovery and development of the G-rich oligonucleotide AS1411 as a novel treatment for cancer.Experimental and molecular pathology · 2009Review
- Article
- alpha-Latrotoxin and its receptors.Handbook of experimental pharmacology · 2008Review
- Dimerization of protein tyrosine phosphatase sigma governs both ligand binding and isoform specificity.Molecular and cellular biology · 2007Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Reversible tyrosine phosphorylation, catalyzed by receptor tyrosine kinases and receptor tyrosine phosphatases, plays an essential part in cell signaling during axonal development. Receptor protein tyrosine phosphatase-sigma has been implicated in the growth, guidance and repair of retinal axons. This phosphatase has also been implicated in motor axon growth and innervation. Insect orthologs of receptor protein tyrosine phosphatase-sigma are also implicated in the recognition of muscle target cells. A potential extracellular ligand for vertebrate receptor protein tyrosine phosphatase-sigma has been previously localized in developing skeletal muscle. The identity of this muscle ligand is currently unknown, but it appears to be unrelated to the heparan sulfate ligands of receptor protein tyrosine phosphatase-sigma. In this study, we have used affinity chromatography and tandem MS to identify nucleolin as a binding partner for receptor protein tyrosine phosphatase-sigma in skeletal muscle tissue. Nucleolin, both from tissue lysates and in purified form, binds to receptor protein tyrosine phosphatase-sigma ectodomains. Its expression pattern also overlaps with that of the receptor protein tyrosine phosphatase-sigma-binding partner previously localized in muscle, and nucleolin can also be found in retinal basement membranes. We demonstrate that a significant amount of muscle-associated nucleolin is present on the cell surface of developing myotubes, and that two nucleolin-binding components, lactoferrin and the HB-19 peptide, can block the interaction of receptor protein tyrosine phosphatase-sigma ectodomains with muscle and retinal basement membranes in tissue sections. These data suggest that muscle cell surface-associated nucleolin represents at least part of the muscle binding site for axonal receptor protein tyrosine phosphatase-sigma and that nucleolin may also be a necessary component of basement membrane binding sites of receptor protein tyrosine phosphatase-sigma.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.