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TrkA in vivo function is negatively regulated by ubiquitination.

Kiris E, Wang T, Yanpallewar S, Dorsey S, Becker J, Bavari S, Palko M, Coppola V, Tessarollo L (2014) TrkA in vivo function is negatively regulated by ubiquitination. J Neurosci 34:4090-4098. doi: 10.1523/JNEUROSCI.4294-13.2014 PMID: 24623787

Summary: The high affinity nerve growth factor receptor, trkA, plays an intrinsic role in the regulation of various aspects of the mammalian nervous system. The post-translational attachment of ubiquitin to trkA plays a role in the final disposition and function of many proteins; in this work the authors investigate the result of trkA ubiquitination. By removing a 3 amino acid sequence from the receptor the ubiquitination of TrkA was reduced which resulted in an increase in TrkA protein levels and activity. In mice containing this mutation, the rise in TrkA activity was accompanied by enhanced thermal sensitivity and inflammatory pain. Anti-trkA (Cat. #AB-N03) was used at a concentration of 1:500 in immunohistochemistry.

Related Products: trkA Rabbit Polyclonal (Cat. #AB-N03)

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