Collapsin response mediator protein family

Collapsin response mediator protein family or CRMP family consists of five intracellular phosphoproteins (CRMP-1, CRMP-2, CRMP-3, CRMP4, CRMP5) of similar molecular size (60–66 kDa) and high (50–70%) amino acid sequence identity. CRMPs are predominantly expressed in the nervous system during development and play important roles in axon formation from neurites and in growth cone guidance and collapse through their interactions with microtubules. Cleaved forms of CRMPs have also been linked to neuron degeneration after trauma induced injury.

The modulation of CRMP-2 expression through various pharmaceuticals is a new and expanding area of research. By discovering chemicals that can either increase or decrease CRMP-2 expression, scientists can potentially reduce the effects of neurological diseases such as Alzheimer's disease and Parkinson's disease.

Members of the CRMP family were discovered independently in different species by several groups working in parallel. Among the five members of the family, CRMP-2 was first identified in 1995. Group of researchers led by Goshima found out that CRMP-2 played a role in the transduction of the extracellular Semaphorin 3A (Sema3A), an inhibitory protein for axonal guidance in chick dorsal root ganglion (DRG). The protein was first named as CRMP-62 having a relative molecular mass of 62 kDa and later referred as CRMP-2. Concurrently, a 64 kDa protein named as TOAD-64 for Turned On After Division, was shown to increase significantly during the development of the cortex of the brain. The cDNA sequence of TOAD-64 corresponded to that of rat CRMP-2. In 1996, mouse CRMP-4, often referred to as Ulip for Unc-33 like phosphoprotein, was discovered by Byk and colleagues, using a rabbit polyclonal antiserum which recognized a 64 kDa mouse brain specific phosphoprotein. In the same year, several other studies cloned CRMPs-1-4 in rat and dihydropyrimidinase (DHPase) homologous sequence of CRMPs-1, -2, and -4 in human fetal brain. Finally, in 2000, CRMP-5 was discovered using two-hybrid screenings of brain libraries or purification from a proteic complex. In following researches, CRMPs were studied as target antigens for autoantibodies in various autoimmune neurodegenerative disorders.

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