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Updated: Aug 17, 2026

Modified Yeast-Two-Hybrid System to Identify Proteins Interacting with the Growth Factor Progranulin
Published on: January 17, 2012
Identification of a conserved protein motif in a group of growth factor receptors
1Institut de Physiologie, Faculté de Médicine, Université de Lausanne, Switzerland.
Abstract:
Residues 370-383 (helix C) of the human nerve growth factor receptor (NGF-R) are highly similar to the sequence of the 14 residue wasp toxin, mastoparan. Both regions are predicted to form amphiphilic alpha-helices, as is the amino-terminal region of the third intracytoplasmic loop (i3) of the beta 2-adrenergic receptor (beta 2AR). As both mastoparan and the beta 2AR i3 interact with G-proteins, it is suggested that helix C of the NGF-R may facilitate interactions with a cytoplasmic protein. A similar structural motif was identified in the cytoplasmic domains of a number of other growth factor receptors, suggesting an important role for this motif in signal transduction mechanisms.
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