cystein string protein, Dcsp, l(3)03988, ab49
Gene model reviewed during 5.47
Annotated transcripts do not represent all possible combinations of alternative exons and/or alternative promoters.
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.55
2.9, 2.3 (northern blot)
249, 223 (aa); 34, 32 (kD observed); 27, 24 (kD predicted)
Fatty acylated. Heavily palmitoylated in the cysteine string motif.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Csp using the Feature Mapper tool.
Csp is expressed in central brain neuropils. It is broadly seen in the R1-R6 terminals, but appears especially to line the borders facing the cartridge interior. Using immunoelectron microscopy, Csp is detected in the photoreceptor cells close to the T-bar ribbon surrounded by synaptic vesicles.
In the adult prothorax and neck, Csp immunoreactivity is observed in the type I boutons of motor neurons innervating ventral cervical muscles, prothoracic sternal anterior rotator muscle 31, and prothoracic sternal adductor muscle 33. Csp immunoreactivity is not detected in Type II boutons.
Csp protein is enriched in the neuropil of the larval ventral ganglion, where synapses occur.
Csp protein is detected presynaptically at larval and adult neuromuscular junctions. Synaptic boutons are strongly stained. In the CNS, Synapse rich regions of the neuropil are stained, but the surrounding cell bodies are not. One isoform is detected predominantly in photoreceptor terminals but not at motor nerve terminals. Csp protein is thought to be associated with synaptic vesicles.
GBrowse - Visual display of RNA-Seq signalsView Dmel\Csp in GBrowse 2
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
Source for merge of Csp anon-WO02059370.50 was sequence comparison ( date:051113 ).
Candidate stable intronic sequence RNA (sisRNA) identified within CDS of this gene.
The J-domain of Csp is important for minimising asynchronous release shortly after the evoked EJP.
The J-domain of Csp is important in maintaining normal Ca[2+] resting levels in synaptic terminals.
Mutations in Csp affect calcium secretion coupling of evoked exocytosis but not vesicle recycling.
Fluorescent Ca-sensitive dye, Ca Crimson, is used to monitor presynaptic Ca dynamics.
An analysis of the excitatory postsynaptic currents from depolarized motor nerve terminals leads to the conclusion that Csp protein is involved in neurotransmitter release and helps to synchronise evoked neurotransmitter release at nerve terminals.
Biochemical characterisation of Csp suggests that fatty acyl groups do not form the main anchor of Csp in membranes as the complete removal of this modification does not dissociate Csp from the membrane.
Neuromuscular transmission is impaired presynaptically in Csp mutant larvae. Csp mutations disrupt depolarisation-secretion coupling, depolarisation fails to trigger transmitter release. This disruption explains the cellular basis of the temperature sensitive paralysis of the mutant larvae.
A RNA helicase, member of the DEAD box protein family, is the adjacent transcript unit to Csp that expresses two RNA transcripts.
Csp expression pattern has been studied: MAB ab49 antibodies were used to screen cDNA expression libraries to identify clones coding for recognized protein fragments.