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This review summarizes studies that elucidate the neuroprotective role of Drosophila CSP, which is critical for maintaining neurotransmitter release and preventing neurodegeneration.
these data suggest that CSP promotes synaptic growth and evoked neurotransmitter release by mechanistically independent signaling pathways
study found dHIP14 to be an essential maternal effect gene required for photoreceptor synaptic transmission and for proper in vivo expression of the palmitoylated presynaptic proteins SNAP-25 (show SNAP25 Proteins) and cysteine string protein
Our data indicate that HIP14 (show ZDHHC17 Proteins) controls neurotransmitter release by regulating the trafficking of CSP to synapses.
csp interaction with Hsc 70 (show HSPA8 Proteins) molecular chaperones is vital for regulated secretion in Xenopus oocytes
Phosphorylation of CSP triggers a major conformational switch that modulates its protein interactions.
In fact, DnaJC5 overexpression induced tau release in cells, neurons, and brain tissue, but only when activity of the chaperone Hsc70 (show HSPA8 Proteins) was intact and when tau was able to associate with this chaperone.
This study demonstrated that Neuronal ceroid lipofuscinosis with DNAJC5/CSPalpha mutation has PPT1 pathology and exhibit aberrant protein palmitoylation.
Missense mutations in DNAJC5 does not play a major role in PD in the Chinese population.
Results indicate of a p.L116del mutation in DNAJC5 from families with autosomal dominant Kufs disease.
Palmitoylation-induced aggregation of mutant CSP-alpha proteins may underlie the development of adult-onset neuronal ceroid lipofuscinosis (show CLN6 Proteins)
association of DNAJC5 mutations with autosomal dominant Kufs disease
This is the first replication study of the identification of DNAJC5 as the disease-causing gene for autosomal dominant ANCL. The identification of the novel gene in ANCL will allow us to gain a better understanding of the pathological mechanism of ANCLs
First evidence that CSP and HSP70 (show HSP70 Proteins), and their interactions with MARCKS (show MARCKS Proteins), are involved in mucin (show SLC13A2 Proteins) secretion from airway epithelium.
Csp not only regulates the exit of CFTR from the ER, but this action is accompanied by Hsc70/Hsp70 and CHIP-mediated CFTR degradation.
These data show that neurodegenerative processes associated with lysosomal dysfunction may be presynaptically initiated by a concomitant reduction in alpha-synuclein and CSPalpha levels at nerve terminals.
The mRNA and protein expression of CSP1 (show RCAN1 Proteins) was elevated in 3T3-L1 adipocytes in insulin (show INS Proteins) resistant states caused by high levels of palmitate and chronic insulin (show INS Proteins) exposure.
gamma-Synuclein binds synaptic vesicles but is unable to rescue the phenotype of CSPalpha-deficient mice.
Using hippocampal cultures, study shows that CSPalpha regulates the stability of client proteins and synaptic vesicle number. Analysis of CSPalpha-dynamin 1 (show DNM1 Proteins) interactions reveals unexpectedly that CSPalpha regulates the polymerization of dynamin 1 (show DNM1 Proteins).
Study shows that cysteine string protein-alpha is required to maintain the size of the releasable pool of synaptic vesicles in motorneurons, presumably by conveying stability to SNAP-25 (show SNAP25 Proteins).
findings suggest that the neurodegeneration in CSPalpha KO mice is primarily produced by defective SNAP-25 (show SNAP25 Proteins) function, which causes neurodegeneration by impairing SNARE (show VTI1B Proteins)-complex assembly
Data indicate that Cspalpha interacts with Syt9, and such a complex may be relevant in the calcium-mediated control of a late stage of exocytosis by triggering the specific recruitment of a folding catalyst at the fusion point.
Data show that deletion of CSPalpha produces an abnormal SNAP-25 (show SNAP25 Proteins) conformer that inhibits SNARE (show VTI1B Proteins)-complex formation, and is subject to ubiquitylation and proteasomal degradation.
CSPalpha is not essential for the normal operation of Ca2 (show CA2 Proteins)+ channels or exocytosis but acts as a presynaptic chaperone that maintains continued synaptic function. Its deletion causes postnatal lethality of knockout mice.
Tonically active ribbon synapses in retina are particularly sensitive to the deletion of CSPalpha and that expression of at least one CSP isoform is essential to protect such tonically active synapses from neurodegeneration.
This gene is a member of the J protein family. J proteins function in many cellular processes by regulating the ATPase activity of 70 kDa heat shock proteins. The encoded protein plays a role in membrane trafficking and protein folding, and has been shown to have anti-neurodegenerative properties. The encoded protein is known to play a role in cystic fibrosis and Huntington's disease. A pseudogene of this gene is located on the short arm of chromosome 8.
, cystein string protein
, cysteine string protein
, cysteine string protein 3
, cysteine-string protein
, DnaJ (Hsp40) homolog, subfamily C, member 5
, cysteine string protein alpha
, dnaJ homolog subfamily C member 5