Abstract.
Collapsin response mediator protein-2 (CRMP-2) plays a crucial role in axonal guidance and neurite outgrowth during neural development and regeneration. We have studied the interaction between calmodulin (CaM) and CRMP-2 and how Ca2+/CaM binding modulates the biological functions of CRMP-2. We have shown that CRMP-2 binds to CaM directly in a Ca2+-dependent manner. The CaM binding site of CRMP-2 is proposed to reside in the last helix of the folded domain, and in line with this, a synthesized peptide representing this helix bound to CaM. In addition, CaM binding inhibits a homotetrameric assembly of CRMP-2 and attenuates calpainmediated CRMP-2 proteolysis. Furthermore, a CaM antagonist reduces the number and length of process induced by CRMP-2 overexpression in HEK293 cells. Take together, our data suggest that CRMP-2 is a novel CaM-binding protein and that CaM binding may play an important role in regulating CRMP-2 functions.
Similar content being viewed by others
Author information
Authors and Affiliations
Corresponding authors
Additional information
Received 26 June 2008; received after revision 18 November 2008; accepted 24 November 2008
Rights and permissions
About this article
Cite this article
Zhang, Z., Majava, V., Greffier, A. et al. Collapsin response mediator protein-2 is a calmodulin-binding protein. Cell. Mol. Life Sci. 66, 526 (2009). https://doi.org/10.1007/s00018-008-8362-1
Published:
DOI: https://doi.org/10.1007/s00018-008-8362-1