Widespread expression of human cysteine string proteins

@article{Coppola1996WidespreadEO,
  title={Widespread expression of human cysteine string proteins},
  author={Thierry Coppola and Cameron B. Gundersen},
  journal={FEBS Letters},
  year={1996},
  volume={391}
}
Wide distribution of the cysteine string proteins in Drosophila tissues revealed by targeted mutagenesis
TLDR
The wide expression of CSPs suggests that at least some of the various phenotypes of the null mutants observed at permissive temperatures, such as delayed development, short adult lifespan, modified electroretinogram, and optomotor behavior, may be caused by the lack of C SPs outside synaptic terminals.
Cysteine string proteins
Characterisation of a new human and murine member of the DnaJ family of proteins.
TLDR
The characterisation of a human gene, designated MCG18 (multiple endocrine neoplasia type 1 candidate gene 18), that encodes a new member of the DnaJ family of proteins, predicted to encode a 241 amino acid product that has partial homology to Escherichia coli dnaJ.
Structure–function analysis of the cysteine string protein in Drosophila: cysteine string, linker and C terminus
TLDR
It is proposed that the cysteine string, in addition to its role in targeting, may be essential for a function of CSP that is dependent on the number of cysteines in the string.
Cysteine‐String Protein
TLDR
Evidence implicate Csps as molecular chaperones in the synapse that are likely to control the correct conformational folding of one or more components of the vesicular exocytotic machinery.
The Molecular Chaperone Function of the Secretory Vesicle Cysteine String Proteins*
TLDR
Results show that both Csp1 and Csp2 can bind a partially unfolded protein and act as chaperones, suggesting that Csps may have a general chaperone function in regulated exocytosis.
Genetic mapping of the gene encoding cysteine string protein
TLDR
The mapping of the porcine NFI/CTF gene to SSC 2q 12-13 corroborates the conserved synteny between HSA19p and the homologous segment at SSC2cen-q21, which has also been demonstrated by a recent forward and reverse Zoo-FISH approach.
Mutational analysis of cysteine-string protein function in insulin exocytosis.
TLDR
A functional difference between the two isoforms of Csp wild-type or mutants is demonstrated and a role for the J-domain co-chaperone function as well as for the newly defined linker region in LDCV exocytosis is suggested.
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References

SHOWING 1-10 OF 22 REFERENCES
Identification of a Novel Cysteine String Protein Variant and Expression of Cysteine String Proteins in Non-neuronal Cells (*)
TLDR
It is suggested that Csps may have a more general role in membrane traffic in non-neuronal as well as neuronal cells after the cloning of two Csp variants from bovine adrenal medullary chromaffin cells.
A cysteine-string protein is expressed in retina and brain of Drosophila.
TLDR
A monoclonal antibody MAB ab49 from a hybridoma library screened for immunohistochemical staining in the adult nervous system of Drosophila melanogaster was found to selectively bind to all neuropil regions and to synaptic boutons of motor neurons.
Antipeptide Antibodies Against a Torpedo Cysteine‐String Protein
TLDR
Results indicate that csp immunoreactivity is detectably expressed in electroplax, a heavily innervated tissue, but not in liver, which should have an appreciably lower abundance of presynaptic calcium channel proteins.
Extensive lipidation of a Torpedo cysteine string protein.
TLDR
Investigations revealed an unprecedented degree of lipidation of these cysteine residues of the Torpedo protein, which makes them candidates to participate in exocytotic membrane fusion.
Cysteine string protein immunoreactivity in the nervous system and adrenal gland of rat
TLDR
The presence of cysteine string proteins in the adrenal medulla suggests that these proteins may also participate in secretion-related events in certain non-neuronal cells.
Eukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteins.
TLDR
New data is presented that indicates that E. coli strains deficient in either dnaK or dnaJ overexpress other heat shock inducible proteins (such as the chaperonin groEL and groES) and are incompetent for phage replication at any temperature (for reviews see Georgopoulos et al, 1990, Ang et al., 1991).
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