Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Synapsins”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 397 records · Page 22Linked to original sources
PubMed1983

A multifunctional calmodulin-dependent protein kinase. Similarities between skeletal muscle glycogen synthase kinase and a brain synapsin I kinase.

Calmodulin-dependent glycogen synthase kinase isolated from skeletal muscle and synapsin I kinase II isolated from brain have several properties that are very similar. These properties include: substrate and site-specificities, immunological cross-reactivity, and phosphopeptide maps following limited proteolysis. Both enzymes phosphorylate a wide variety of substrate proteins. The two kinases may represent different isozymes of a multifunctional calmodulin-dependent protein kinase that mediates many of the actions of Ca2+ in various tissues. Therefore, we propose the name 'calmodulin-dependent multi-protein kinase' for this broad specificity enzyme.

Animals↗
PubMed1991

Polyphosphoinositides as activators of PKC-dependent synapsin I phosphorylation.

The effect of PIP2 and diacylglycerol (products of polyphosphoinositide turnover) on the activation level of phosphorylation of the human brain neurospecific protein SI by PKC from the same source was studied. The apparent activation constant of the phosphorylation process was shown to decrease in the presence of PIP2 from 1.1 micrograms/ml for PI and from 0.8 micrograms/ml to 0.6 microgram/ml for PS; the value of 0.4 microgram/ml in the latter case was detected merely after the addition of DOG into the reaction mixture. Polyphosphoinositides are suggested to play a role in activating PKC-mediated phosphorylation of SI in nerve terminals.

Humans↗
PubMed2004

Identification of a novel brain-specific and Reelin-regulated gene that encodes a protein colocalized with synapsin.

We carried out a screening of genes that are differentially expressed in normal mice and reeler mutants and are characterized by abnormal neuronal migration and neurite deployment due to defective Reelin signalling. A novel gene, provisionally named C61, was overexpressed in Reelin-deficient embryonic mouse brain RNA. C61 encodes a 3.7 kb mRNA that is brain specific and developmentally regulated, with predominant expression in differentiating neurons. The predicted protein is 664 amino acids long, and contains LAG1 and Ezrin/Radixin/Moesin-Myosin-Filament motifs, suggesting that it may function as an intracellular adaptor. From E14.5 to birth, C61 was highly expressed in all neuronal differentiation fields, with the highest signal in the telencephalic cortical plate and mitral cells in the olfactory bulb. When expressed as a GFP fusion protein in transfected non-neuronal cells and primary neurons, this protein localizes, respectively, to the nuclear membrane or axonal outgrowths, indicating a function in axonal traffic or signalling.

Amino Acid Motifs↗