Synapsin I (protein I), a nerve terminal-specific phosphoprotein. III. Its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation.
Synapsin I (protein I), a nerve terminal-specific phosphoprotein. III. Its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation.
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DOI：
10.1083/jcb.96.5.1374
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发表时间：
1983-05
期刊：
影响因子：
--
通讯作者：
De Camilli P
中科院分区：
文献类型：
--
作者：
Huttner WB;Schiebler W;Greengard P;De Camilli P
Synapsin I (protein I) is a neuron-specific phosphoprotein, which is a substrate for cAMP-dependent and Ca/calmodulin-dependent protein kinases. In two accompanying studies (De Camilli, P., R. Cameron, and P. Greengard, and De Camilli, P., S. M. Harris, Jr., W. B. Huttner, and P. Greengard, 1983, J. Cell Biol. 96:1337-1354 and 1355-1373) we have shown, by immunocytochemical techniques at the light microscopic and electron microscopic levels, that synapsin I is present in the majority of, and possibly in all, nerve terminals, where it is primarily associated with synaptic vesicles. In the present study we have prepared a highly purified synaptic vesicle fraction from rat brain by a procedure that involves permeation chromatography on controlled-pore glass as a final purification step. Using immunological methods, synapsin I concentrations were determined in various subcellular fractions obtained in the course of vesicle purification. Synapsin I was found to copurify with synaptic vesicles and to represent approximately 6% of the total protein in the highly purified synaptic vesicle fraction. The copurification of synapsin I with synaptic vesicles was dependent on the use of low ionic strength media throughout the purification. Synapsin I was released into the soluble phase by increased ionic strength at neutral pH, but not by nonionic detergents. The highly purified synaptic vesicle fraction contained a calcium-dependent protein kinase that phosphorylated endogenous synapsin I in its collagenase-sensitive tail region. The phosphorylation of this region appeared to facilitate the dissociation of synapsin I from synaptic vesicles under the experimental conditions used.
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DOI：
10.1083/jcb.74.1.181
发表时间：
1977-07
期刊：
The Journal of cell biology
影响因子：
--
作者：
Cohen RS;Blomberg F;Berzins K;Siekevitz P
通讯作者：
Siekevitz P
DOI：
10.1073/pnas.77.12.7487
发表时间：
1980-01-01
期刊：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES
影响因子：
--
作者：
KACZMAREK, LK;JENNINGS, KR;GREENGARD, P
通讯作者：
GREENGARD, P
影响因子：
5.6
作者：
PEARSE, BMF
通讯作者：
PEARSE, BMF
影响因子：
64.8
作者：
NESTLER, EJ;GREENGARD, P
通讯作者：
GREENGARD, P
DOI：
10.1073/pnas.76.11.5982
发表时间：
1979-01-01
影响因子：
11.1
作者：
BLOOM, FE;UEDA, T;GREENGARD, P
通讯作者：
GREENGARD, P