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The Journal of Neuroscience, March 17, 2004, 24(11):2742-2749; doi:10.1523/JNEUROSCI.3960-03.2004

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Cellular/Molecular
A Novel p75 Neurotrophin Receptor-Related Protein, NRH2, Regulates Nerve Growth Factor Binding to the TrkA Receptor

Simon S. Murray,¹ Pilar Perez,³ Ramee Lee,² Barbara L. Hempstead,² and Moses V. Chao¹

¹Skirball Institute of Bimolecular Medicine, New York University School of Medicine, New York, New York 10016, ²Division of Hematology, Weill Medical College of Cornell University, New York, New York 10021, and ³Instituto de Microbiologia Bioquimica, Departamento de Microbiologia y Genetica, Consejo Superior de Investigaciones Científicas, Universidad de Salamanca, 37007 Salamanca, Spain

Nerve growth factor (NGF) functions as a ligand for two receptors, the TrkA tyrosine kinase receptor and the p75 neurotrophin receptor (p75^NTR). The Ig-like domains of Trk receptors and the cysteine-rich repeats of p75^NTR are involved in binding to the neurotrophins. Recently, a closely related gene to p75^NTR called neurotrophin receptor homolog-2 (NRH2) was identified; however, the function of NRH2 and its relevance to neurotrophin signaling are unclear. NRH2 contains a similar transmembrane and intracellular domain as p75^NTR but lacks the characteristic cysteine-rich repeats in the extracellular domain. Here we show that NRH2 is expressed in several neuronal populations that also express p75^NTR and Trk receptors. NRH2 does not bind to NGF; however, coimmunoprecipitation experiments demonstrate that NRH2 is capable of interacting with TrkA receptors. Coexpression of NRH2 with TrkA receptors resulted in the formation of high-affinity binding sites for NGF. These results indicate that a transmembrane protein related to p75^NTR is capable of modulating Trk receptor binding properties.

Key words: neurotrophin; receptor; high-affinity binding; p75; NGF; Trk

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Received Aug 27, 2003; revised December 3, 2003; accepted January 12, 2004.

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