TY - JOUR
T1 - Wide distribution of the cysteine string proteins in Drosophila tissues revealed by targeted mutagenesis
AU - Eberle, Kai K.
AU - Zinsmaier, Konrad E.
AU - Buchner, Sigrid
AU - Gruhn, Matthias
AU - Jenni, Mario
AU - Arnold, Christine
AU - Leibold, Christian
AU - Reisch, Dietmar
AU - Walter, Nik
AU - Hafen, Ernst
AU - Hofbauer, Alois
AU - Pflugfelder, Gert O.
AU - Buchner, Erich
N1 - Funding Information:
Supported by Deutsche Forschungsgemeinschaft (DFG) grants Bu566/1,6 to E.B. and a postdoctoral DFG grant to K.E.Z.
PY - 1998
Y1 - 1998
N2 - The 'cysteine string protein' (CSP) genes of higher eukaryotes code for a novel family of proteins characterized by a 'J' domain and an unusual cysteine-rich region. Previous studies had localized the proteins in neuropil and synaptic terminals of larval and adult Drosophila and linked the temperature-sensitive paralysis of the mutants described here to conditional failure of synaptic transmission. We now use the null mutants as negative controls in order to reliably detect even low concentrations of CSPs by immunohistochemistry, employing three monoclonal antibodies. In wild-type flies high levels of cysteine string proteins are found not only in apparently all synaptic terminals of the embryonic, larval, and adult nervous systems, but also in the 'tall cells' of the cardia, in the follicle cells of the ovary, in specific structures of the female spermatheca, and in the male testis and ejaculatory bulb. In addition, low levels of CSPs appear to be present in all tissues examined, including neuronal perikarya, axons, muscles, Malpighian tubules, and salivary glands. Western blots of isolated tissues demonstrate that of the four isoforms expressed in heads only the largest is found in non-neural organs. 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 CSPs outside synaptic terminals.
AB - The 'cysteine string protein' (CSP) genes of higher eukaryotes code for a novel family of proteins characterized by a 'J' domain and an unusual cysteine-rich region. Previous studies had localized the proteins in neuropil and synaptic terminals of larval and adult Drosophila and linked the temperature-sensitive paralysis of the mutants described here to conditional failure of synaptic transmission. We now use the null mutants as negative controls in order to reliably detect even low concentrations of CSPs by immunohistochemistry, employing three monoclonal antibodies. In wild-type flies high levels of cysteine string proteins are found not only in apparently all synaptic terminals of the embryonic, larval, and adult nervous systems, but also in the 'tall cells' of the cardia, in the follicle cells of the ovary, in specific structures of the female spermatheca, and in the male testis and ejaculatory bulb. In addition, low levels of CSPs appear to be present in all tissues examined, including neuronal perikarya, axons, muscles, Malpighian tubules, and salivary glands. Western blots of isolated tissues demonstrate that of the four isoforms expressed in heads only the largest is found in non-neural organs. 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 CSPs outside synaptic terminals.
KW - 'J' domain
KW - Calcium channel
KW - Chaperone
KW - Drosophila melanogaster (Insecta)
KW - Exocytosis
KW - Gene knock-out
KW - Temperature-sensitive paralysis
UR - http://www.scopus.com/inward/record.url?scp=15644376734&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=15644376734&partnerID=8YFLogxK
U2 - 10.1007/s004410051170
DO - 10.1007/s004410051170
M3 - Article
C2 - 9799436
AN - SCOPUS:15644376734
SN - 0302-766X
VL - 294
SP - 203
EP - 217
JO - Cell and Tissue Research
JF - Cell and Tissue Research
IS - 2
ER -