Collapsin response mediator protein-2 is a calmodulin-binding protein |
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| Authors: | Z Zhang V Majava A Greffier R L Hayes P Kursula K K W Wang |
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| Institution: | (1) Center of Innovative Research, Banyan Biomarkers Inc, 12805 Research Drive, Alachua, FL 32615, USA;(2) Department of Biochemistry, University of Oulu, Oulu, Finland;(3) Department of Anesthesiology, McKnight Brain Institute of the University of Florida, Gainesville, FL, USA;(4) Department of Psychiatry, McKnight Brain Institute of the University of Florida, Gainesville, FL, USA |
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| 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.
Received 26 June 2008; received after revision 18 November 2008; accepted 24 November 2008 |
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| Keywords: | " target="_blank"> CRMP-2 proteolysis calmodulin calmodulin-binding protein oligomerization |
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