Cryptochrome structure and signal transduction

Annu Rev Plant Biol. 2003;54:469-96. doi: 10.1146/annurev.arplant.54.110901.160901.


Cryptochromes are photosensory receptors mediating light regulation of growth and development in plants. Since the isolation of the Arabidopsis CRY1 gene in 1993, cryptochromes have been found in every multicellular eukaryote examined. Most plant cryptochromes have a chromophore-binding domain that shares similar structure with DNA photolyase, and a carboxyl terminal extension that contains a DQXVP-acidic-STAES (DAS) domain conserved from moss, to fern, to angiosperm. In Arabidopsis, cryptochromes are nuclear proteins that mediate light control of stem elongation, leaf expansion, photoperiodic flowering, and the circadian clock. Cryptochromes may act by interacting with proteins such as phytochromes, COP1, and clock proteins, or/and chromatin and DNA. Recent studies suggest that cryptochromes undergo a blue light-dependent phosphorylation that affects the conformation, intermolecular interactions, physiological activities, and protein abundance of the photoreceptors.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Cryptochromes
  • Cytochromes / metabolism
  • Deoxyribodipyrimidine Photo-Lyase / genetics
  • Drosophila Proteins*
  • Eye Proteins*
  • Flavoproteins / chemistry*
  • Flavoproteins / genetics
  • Flavoproteins / physiology
  • Molecular Sequence Data
  • Multigene Family
  • Photoreceptor Cells, Invertebrate*
  • Plant Physiological Phenomena
  • Plant Proteins / metabolism
  • Plants / genetics
  • Receptors, G-Protein-Coupled
  • Signal Transduction / physiology*


  • Cryptochromes
  • Cytochromes
  • Drosophila Proteins
  • Eye Proteins
  • Flavoproteins
  • Plant Proteins
  • Receptors, G-Protein-Coupled
  • cry protein, Drosophila
  • Deoxyribodipyrimidine Photo-Lyase