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| Subject Categories: Membranes & Transport | Signal Transduction |
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| The EMBO Journal
(2003) 22, 1790–1800, doi:10.1093/emboj/cdg177 |
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| PKA phosphorylates the p75 receptor and regulates its localization to lipid rafts |
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| Haruhisa Higuchi1, 2, 3, Toshihide Yamashita1, 3, Hideki Yoshikawa2 and Masaya Tohyama1, 3 |
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1 Department of Anatomy and Neuroscience Graduate School of Medicine, Osaka University, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan 2 Department of Orthopaedic Surgery, Graduate School of Medicine, Osaka University, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan 3 CREST, Japan Science and Technology Corporation, 4-1-8 Honmachi, Kawaguchi, Saitama 332-0012, Japan To whom correspondence should be addressed Toshihide Yamashita, tyama@anat2.med.osaka-u.ac.jp Received 28 November 2002; Revised 20 February 2003; Accepted 24 February 2003. |
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| Abstract |
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Although a large number of studies have been carried out on the diverse effects mediated by the common neurotrophin receptor p75NTR, little is known about the molecular mechanisms by which p75NTR initiates intracellular signal transduction. We identified a variant of the  catalytic subunit of cAMP-dependent protein kinase (PKAC) as a p75NTR-interacting protein, which phosphorylates p75NTR at Ser304. Intracellular cAMP in cerebellar neurons was accumulated transiently by ligand binding to p75NTR. Activation of cAMP-PKA is required for translocation of p75NTR to lipid rafts, and for biochemical and biological activities of p75NTR, such as inactivation of Rho and the neurite outgrowth. Proper recruitment of activated p75NTR to lipid rafts, structures that represent specialized signaling organelles, is of fundamental importance in determining p75NTR bioactivity. |
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| Keywords: lipid raft, neuron, p75NTR, PKA, splice variant |
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