scholarly journals O-Linked β-N-Acetylglucosamine (O-GlcNAc) Site Thr-87 Regulates Synapsin I Localization to Synapses and Size of the Reserve Pool of Synaptic Vesicles

2013 ◽  
Vol 289 (6) ◽  
pp. 3602-3612 ◽  
Author(s):  
Yuliya Skorobogatko ◽  
Ashly Landicho ◽  
Robert J. Chalkley ◽  
Andrew V. Kossenkov ◽  
Gianluca Gallo ◽  
...  
Keyword(s):  
Synaptic Vesicles ◽  
Synapsin I ◽  
Reserve Pool

scholarly journals Intersectin associates with synapsin and regulates its nanoscale localization and function

2017 ◽  
Vol 114 (45) ◽  
pp. 12057-12062 ◽  
Author(s):  
Fabian Gerth ◽  
Maria Jäpel ◽  
Arndt Pechstein ◽  
Gaga Kochlamazashvili ◽  
Martin Lehmann ◽  
...  
Keyword(s):  
Synaptic Vesicles ◽  
Synapsin I ◽  
Wild Type ◽  
Src Homology 3 ◽  
Reserve Pool ◽  
Hippocampal Synapses ◽  
Important Regulator ◽  
Src Homology ◽  
Elevated Activity ◽  
And Function

Neurotransmission is mediated by the exocytic release of neurotransmitters from readily releasable synaptic vesicles (SVs) at the active zone. To sustain neurotransmission during periods of elevated activity, release-ready vesicles need to be replenished from the reserve pool of SVs. The SV-associated synapsins are crucial for maintaining this reserve pool and regulate the mobilization of reserve pool SVs. How replenishment of release-ready SVs from the reserve pool is regulated and which other factors cooperate with synapsins in this process is unknown. Here we identify the endocytic multidomain scaffold protein intersectin as an important regulator of SV replenishment at hippocampal synapses. We found that intersectin directly associates with synapsin I through its Src-homology 3 A domain, and this association is regulated by an intramolecular switch within intersectin 1. Deletion of intersectin 1/2 in mice alters the presynaptic nanoscale distribution of synapsin I and causes defects in sustained neurotransmission due to defective SV replenishment. These phenotypes were rescued by wild-type intersectin 1 but not by a locked mutant of intersectin 1. Our data reveal intersectin as an autoinhibited scaffold that serves as a molecular linker between the synapsin-dependent reserve pool and the presynaptic endocytosis machinery.

scholarly journals Characterization of synapsin I binding to small synaptic vesicles.

1986 ◽  
Vol 261 (18) ◽  
pp. 8383-8390
Author(s):  
W Schiebler ◽  
R Jahn ◽  
J P Doucet ◽  
J Rothlein ◽  
P Greengard
Keyword(s):  
Synaptic Vesicles ◽  
Synapsin I

scholarly journals Kinetic analysis of the phosphorylation-dependent interactions of synapsin I with rat brain synaptic vesicles

1997 ◽  
Vol 504 (3) ◽  
pp. 501-515 ◽  
Author(s):  
Giovanni Stefani ◽  
Franco Onofri ◽  
Flavia Valtorta ◽  
Paola Vaccaro ◽  
Paul Greengard ◽  
...  
Keyword(s):  
Kinetic Analysis ◽  
Rat Brain ◽  
Synaptic Vesicles ◽  
Synapsin I

scholarly journals Interactions of synapsin I with phospholipids: possible role in synaptic vesicle clustering and in the maintenance of bilayer structures.

1993 ◽  
Vol 123 (6) ◽  
pp. 1845-1855 ◽  
Author(s):  
F Benfenati ◽  
F Valtorta ◽  
M C Rossi ◽  
F Onofri ◽  
T Sihra ◽  
...  
Keyword(s):  
Synaptic Vesicle ◽  
Synaptic Vesicles ◽  
High Surface ◽  
Resonance Spectroscopy ◽  
Synapsin I ◽  
Hydrophobic Core ◽  
Membrane Phospholipids ◽  
Head Region ◽  
Vesicle Membrane ◽  
Liposome Fusion

Synapsin I is a synaptic vesicle-specific phosphoprotein composed of a globular and hydrophobic head and of a proline-rich, elongated and basic tail. Synapsin I binds with high affinity to phospholipid and protein components of synaptic vesicles. The head region of the protein has a very high surface activity, strongly interacts with acidic phospholipids and penetrates the hydrophobic core of the vesicle membrane. In the present paper, we have investigated the possible functional effects of the interaction between synapsin I and vesicle phospholipids. Synapsin I enhances both the rate and the extent of Ca(2+)-dependent membrane fusion, although it has no detectable fusogenic activity per se. This effect, which appears to be independent of synapsin I phosphorylation and localized to the head region of the protein, is attributable to aggregation of adjacent vesicles. The facilitation of Ca(2+)-induced liposome fusion is maximal at 50-80% of vesicle saturation and then decreases steeply, whereas vesicle aggregation does not show this biphasic behavior. Association of synapsin I with phospholipid bilayers does not induce membrane destabilization. Rather, 31P-nuclear magnetic resonance spectroscopy demonstrated that synapsin I inhibits the transition of membrane phospholipids from the bilayer (L alpha) to the inverted hexagonal (HII) phase induced either by increases in temperature or by Ca2+. These properties might contribute to the remarkable selectivity of the fusion of synaptic vesicles with the presynaptic plasma membrane during exocytosis.

Sign in / Sign up

Export Citation Format

Share Document