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Gene Review:

cby1 - chibby homolog 1

Xenopus laevis

Synonyms: arb1, cby, chibby, pgea1, pigea-14, ...

Fukuda, M. et al., Windisch, J.M. et al., Haines, B.P. et al., Heger, P. et al., Daher, W. et al., et al.

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High impact information on LOC398327

CRM1 is an export receptor for leucine-rich nuclear export signals [1].
Although the consensus motif of the NESs has been shown to be a leucine-rich, short amino-acid sequence, its receptor has not been identified [2].
Regulation of protein phosphatase type 1 and cell cycle progression by PfLRR1, a novel leucine-rich repeat protein of the human malaria parasite Plasmodium falciparum [3].
Here we describe a new evolutionarily conserved motif within zinc finger proteins which we have named the leucine rich region (LeR) [4].
Within the mammalian genome, there are many multimember gene families that encode membrane proteins with extracellular leucine rich repeats which are thought to act as cell adhesion or signalling molecules [5].

Biological context of LOC398327

With 24 amino acids determining the affinities and kinetics of the interactions with three different partners, the leucine-rich motif is strongly established as one of the most potent and flexible protein--protein interaction motifs [6].

Associations of LOC398327 with chemical compounds

We also show that nuclear export of a fission yeast protein, Dsk1, which has a leucine-rich NES, is disrupted in wild-type yeast treated with LMB or in the crm1 mutant [2].

Analytical, diagnostic and therapeutic context of LOC398327

Using microinjection of defined recombinant export substrates, we now demonstrate that leucine-rich nuclear export signals varied dramatically in determining the kinetics of export in vivo [7].

References

CRM1 is an export receptor for leucine-rich nuclear export signals. Fornerod, M., Ohno, M., Yoshida, M., Mattaj, I.W. Cell (1997) [Pubmed]
CRM1 is responsible for intracellular transport mediated by the nuclear export signal. Fukuda, M., Asano, S., Nakamura, T., Adachi, M., Yoshida, M., Yanagida, M., Nishida, E. Nature (1997) [Pubmed]
Regulation of protein phosphatase type 1 and cell cycle progression by PfLRR1, a novel leucine-rich repeat protein of the human malaria parasite Plasmodium falciparum. Daher, W., Browaeys, E., Pierrot, C., Jouin, H., Dive, D., Meurice, E., Dissous, C., Capron, M., Tomavo, S., Doerig, C., Cailliau, K., Khalife, J. Mol. Microbiol. (2006) [Pubmed]
Repression of transcriptional activity at a distance by the evolutionarily conserved KRAB domain present in a subfamily of zinc finger proteins. Pengue, G., Calabrò, V., Bartoli, P.C., Pagliuca, A., Lania, L. Nucleic Acids Res. (1994) [Pubmed]
Regulated expression of FLRT genes implies a functional role in the regulation of FGF signalling during mouse development. Haines, B.P., Wheldon, L.M., Summerbell, D., Heath, J.K., Rigby, P.W. Dev. Biol. (2006) [Pubmed]
Brain-derived neurotrophic factor, neurotrophin-3, and neurotrophin-4 bind to a single leucine-rich motif of TrkB. Windisch, J.M., Marksteiner, R., Lang, M.E., Auer, B., Schneider, R. Biochemistry (1995) [Pubmed]
Qualitative highly divergent nuclear export signals can regulate export by the competition for transport cofactors in vivo. Heger, P., Lohmaier, J., Schneider, G., Schweimer, K., Stauber, R.H. Traffic (2001) [Pubmed]

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