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Gene Review

Csp  -  Cysteine string protein

Drosophila melanogaster

Synonyms: CG6395, CSP, CSP32, Cys, D-CSP, ...
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Disease relevance of Csp

  • The deduced amino-acid (aa) sequence shows strong similarities with Ip peptides from Escherichia coli, yeasts, plants and mammals, with 100% aa identity around the three Cys clusters which form the non-heme iron-sulfur centers [1].
  • We have found that the previously identified Cys-rich central region contains multiple novel zinc finger motifs which are also present in the Polycomb-like protein and RBP2, a retinoblastoma binding protein [2].

Psychiatry related information on Csp

  • Csp mutants that could generate patterned motor activity had slower, poorly coordinated rhythms with altered temperature sensitivity [3].

High impact information on Csp

  • We suggest that Hsc4 and CSP cooperatively augment the probability of release by increasing the Ca(2+) sensitivity of vesicle fusion [4].
  • The predicted odd protein of 392 amino acids is highly basic and contains four tandem Cys-Cys/His-His zinc finger repeats, consistent with a presumed function for odd as a DNA binding protein and transcriptional regulator [5].
  • Here we show that the serine residues flanking the C-terminal Cys residues of Drosophila TrxRs are responsible for activating the cysteines to match the catalytic efficiency of a selenocysteine-cysteine pair as in mammalian TrxR, obviating the need for selenium [6].
  • The amino acid sequence (2547 residues) of the complete open reading frame of the X gene has 44% identity and 88% similarity to the Drosophila sequence and contains the conserved Cys and His domains characteristic of deubiquitinating enzymes, suggesting its biochemical function may be the hydrolysis of ubiquitin from protein-ubiquitin conjugates [7].
  • Increased Ca(2+) signals coupled with reduced release suggest a direct function of CSP in exocytosis downstream from Ca(2+) entry [8].

Biological context of Csp


Anatomical context of Csp


Associations of Csp with chemical compounds

  • Likewise, 4-aminopyridine, which augments transmitter release at permissive temperature in csp mutants, fails to reverse the inhibition of impulse-evoked transmitter release at elevated temperature [12].
  • No intermediate with an NH2-terminal Cys or Met could be demonstrated [15].
  • In contrast, the Cys homolog of Drosophila melanogaster exhibits a clear preference for Trx, the net forward rate constant, k'(+2), for reduction by Trx being 1.5x10(6) M(-1) s(-1), but only 5.4 M(-1) s(-1) for glutathione [16].
  • Virtually all BIRs contain three Cys and a His that bind zinc, a Gly in a tight turn, and an Arg [17].
  • Classic performic acid oxidation modifies three residues, Cys to CysO(3), Met to MetO(2), and Trp to TrpO(2) [18].


  1. Characterization of the gene encoding the iron-sulfur protein subunit of succinate dehydrogenase from Drosophila melanogaster. Au, H.C., Scheffler, I.E. Gene (1994) [Pubmed]
  2. The Drosophila trithorax proteins contain a novel variant of the nuclear receptor type DNA binding domain and an ancient conserved motif found in other chromosomal proteins. Stassen, M.J., Bailey, D., Nelson, S., Chinwalla, V., Harte, P.J. Mech. Dev. (1995) [Pubmed]
  3. Impairment of central pattern generation in Drosophila cysteine string protein mutants. Barclay, J.W., Atwood, H.L., Robertson, R.M. Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology. (2002) [Pubmed]
  4. Drosophila Hsc70-4 is critical for neurotransmitter exocytosis in vivo. Bronk, P., Wenniger, J.J., Dawson-Scully, K., Guo, X., Hong, S., Atwood, H.L., Zinsmaier, K.E. Neuron (2001) [Pubmed]
  5. Molecular analysis of odd-skipped, a zinc finger encoding segmentation gene with a novel pair-rule expression pattern. Coulter, D.E., Swaykus, E.A., Beran-Koehn, M.A., Goldberg, D., Wieschaus, E., Schedl, P. EMBO J. (1990) [Pubmed]
  6. Active sites of thioredoxin reductases: why selenoproteins? Gromer, S., Johansson, L., Bauer, H., Arscott, L.D., Rauch, S., Ballou, D.P., Williams, C.H., Schirmer, R.H., Arnér, E.S. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  7. The Drosophila developmental gene fat facets has a human homologue in Xp11.4 which escapes X-inactivation and has related sequences on Yq11.2. Jones, M.H., Furlong, R.A., Burkin, H., Chalmers, I.J., Brown, G.M., Khwaja, O., Affara, N.A. Hum. Mol. Genet. (1996) [Pubmed]
  8. Cysteine-string protein increases the calcium sensitivity of neurotransmitter exocytosis in Drosophila. Dawson-Scully, K., Bronk, P., Atwood, H.L., Zinsmaier, K.E. J. Neurosci. (2000) [Pubmed]
  9. Cysteine-string protein: the chaperone at the synapse. Chamberlain, L.H., Burgoyne, R.D. J. Neurochem. (2000) [Pubmed]
  10. Evidence for a diverse Cys-loop ligand-gated ion channel superfamily in early bilateria. Dent, J.A. J. Mol. Evol. (2006) [Pubmed]
  11. A cysteine-string protein is expressed in retina and brain of Drosophila. Zinsmaier, K.E., Hofbauer, A., Heimbeck, G., Pflugfelder, G.O., Buchner, S., Buchner, E. J. Neurogenet. (1990) [Pubmed]
  12. Evidence that cysteine string proteins regulate an early step in the Ca2+-dependent secretion of neurotransmitter at Drosophila neuromuscular junctions. Umbach, J.A., Gundersen, C.B. J. Neurosci. (1997) [Pubmed]
  13. A mutation affecting dihydropyridine-sensitive current levels and activation kinetics in Drosophila muscle and mammalian heart calcium channels. Ren, D., Xu, H., Eberl, D.F., Chopra, M., Hall, L.M. J. Neurosci. (1998) [Pubmed]
  14. Cysteine string protein is required for calcium secretion coupling of evoked neurotransmission in drosophila but not for vesicle recycling. Ranjan, R., Bronk, P., Zinsmaier, K.E. J. Neurosci. (1998) [Pubmed]
  15. NH2-terminal processing of Drosophila melanogaster actin. Sequential removal of two amino acids. Rubenstein, P.A., Martin, D.J. J. Biol. Chem. (1983) [Pubmed]
  16. The Thioredoxin Specificity of Drosophila GPx: A Paradigm for a Peroxiredoxin-like Mechanism of many Glutathione Peroxidases. Maiorino, M., Ursini, F., Bosello, V., Toppo, S., Tosatto, S.C., Mauri, P., Becker, K., Roveri, A., Bulato, C., Benazzi, L., De Palma, A., Floh??, L. J. Mol. Biol. (2007) [Pubmed]
  17. A highly conserved arginine is critical for the functional folding of inhibitor of apoptosis (IAP) BIR domains. Luque, L.E., Grape, K.P., Junker, M. Biochemistry (2002) [Pubmed]
  18. Use of performic acid oxidation to expand the mass distribution of tryptic peptides. Matthiesen, R., Bauw, G., Welinder, K.G. Anal. Chem. (2004) [Pubmed]
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