Interaction of receptor-activity-modifying protein1 with tubulin

Thomas H. Kunz, Sarah Mueller-Steiner, Kerstin Schwerdtfeger, Peter Kleinert, Heinz Troxler, Jens M. Kelm, Lars M. Ittner, Jan A. Fischer, Walter Born*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


Receptor-activity-modifying protein (RAMP) 1 is an accessory protein of the G protein-coupled calcitonin receptor-like receptor (CLR). The CLR/RAMP1 heterodimer defines a receptor for the potent vasodilatory calcitonin gene-related peptide. A wider tissue distribution of RAMP1, as compared to that of the CLR, is consistent with additional biological functions. Here, glutathione S-transferase (GST) pull-down, coimmunoprecipitation and yeast two-hybrid experiments identified β-tubulin as a novel RAMP1-interacting protein. GST pull-down experiments indicated interactions between the N- and C-terminal domains of RAMP1 and β-tubulin. Yeast two-hybrid experiments confirmed the interaction between the N-terminal region of RAMP1 and β-tubulin. Interestingly, α-tubulin was co-extracted with β-tubulin in pull-down experiments and immunoprecipitation of RAMP1 coprecipitated α- and β-tubulin. Confocal microscopy indicated colocalization of RAMP1 and tubulin predominantly in axon-like processes of neuronal differentiated human SH-SY5Y neuroblastoma cells. In conclusion, the findings point to biological roles of RAMP1 beyond its established interaction with G protein-coupled receptors.

Original languageEnglish
Pages (from-to)1145-1150
Number of pages6
JournalBiochimica et Biophysica Acta - General Subjects
Issue number8
Publication statusPublished - 1 Aug 2007
Externally publishedYes


  • β-tubulin
  • Calcitonin gene-related peptide
  • Calcitonin receptor-like receptor
  • Matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS)
  • Protein interaction
  • Receptor-activity-modifying protein

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