Dec 31, 1997

Brain CRMP forms heterotetramers similar to liver dihydropyrimidinase

Journal of Neurochemistry
L H Wang, S M Strittmatter

Abstract

The cytoplasmic collapsin response mediator protein CRMP62 is involved in the signaling cascade initiated by collapsin-1, which collapses neuronal growth cones. To investigate the mechanism of CRMP action, we screened mouse and human fetal cDNA libraries by the yeast two-hybrid method with CRMP as bait. Clones encoding CRMP1 and CRMP4 were isolated, suggesting that the CRMPs form multimers. This finding was confirmed by expressing various rat CRMP cDNAs in the yeast two-hybrid system. Rat CRMP isoforms show differential association with one another. Heterooligomerization is preferred in both two-hybrid and in vitro binding assays. Purified bovine brain CRMP migrates as a tetramer during size exclusion chromatography. Examination of binding with truncated forms of CRMPs indicates that the avid association of CRMPs requires nearly intact proteins. Through the analysis of CRMP chimeras, CRMP amino acids 8-134 and 281-435 are found to be essential for CRMP oligomerization. The tetrameric structure of CRMP resembles that of liver dihydropyrimidinase (DHPase), a protein that shares sequence similarity with the CRMPs. Although purified brain CRMP does not hydrolyze several DHPase substrates, it is likely that a related activity accoun...Continue Reading

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Mentioned in this Paper

Collapsin response mediator protein-2
DPYSL3
Brain
Paracrine Protein Factors
Crmp1
Polymers
Dpysl3
DPYS
Dpysl3
Dihydropyrimidinase

About this Paper

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