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How synapsin I may cluster synaptic vesicles. / Shupliakov, Oleg; Haucke, Volker; Pechstein, Arndt.

In: Seminars in Cell and Developmental Biology, Vol. 22, No. 4, 01.01.2011, p. 393-399.

Research output: Contribution to journal › Review article › peer-review

Harvard

Shupliakov, O, Haucke, V & Pechstein, A 2011, 'How synapsin I may cluster synaptic vesicles', Seminars in Cell and Developmental Biology, vol. 22, no. 4, pp. 393-399. https://doi.org/10.1016/j.semcdb.2011.07.006

APA

Shupliakov, O., Haucke, V., & Pechstein, A. (2011). How synapsin I may cluster synaptic vesicles. Seminars in Cell and Developmental Biology, 22(4), 393-399. https://doi.org/10.1016/j.semcdb.2011.07.006

Vancouver

Shupliakov O, Haucke V, Pechstein A. How synapsin I may cluster synaptic vesicles. Seminars in Cell and Developmental Biology. 2011 Jan 1;22(4):393-399. https://doi.org/10.1016/j.semcdb.2011.07.006

Author

Shupliakov, Oleg ; Haucke, Volker ; Pechstein, Arndt. / How synapsin I may cluster synaptic vesicles. In: Seminars in Cell and Developmental Biology. 2011 ; Vol. 22, No. 4. pp. 393-399.

BibTeX

@article{ab622ad605d24c5291484ef795088978,
title = "How synapsin I may cluster synaptic vesicles",
abstract = "Synapsin I is the most abundant brain phosphoprotein present in conventional synapses of the CNS. Knockout and rescue experiments have demonstrated that synapsin is essential for clustering of synaptic vesicles (SVs) at active zones and the organization of the reserve pool of SVs. However, in spite of intense efforts it remains largely unknown how exactly synapsin I performs this function. It has been proposed that synapsin I in its dephosphorylated state may tether SVs to actin filaments within the cluster from where SVs are released in response to activity-induced synapsin phosphorylation. Recent studies, however, have failed to detect actin filaments inside the vesicle cluster at resting central synapses. Instead, proteins with established functional roles in SV recycling have been found within this presynaptic compartment. Here we discuss potential alternative mechanisms of synapsin I-dependent SV clustering in the reserve pool.",
keywords = "Endocytic proteins, Synapse, Synapsin, Synaptic vesicle, Vesicle clustering",
author = "Oleg Shupliakov and Volker Haucke and Arndt Pechstein",
year = "2011",
month = jan,
day = "1",
doi = "10.1016/j.semcdb.2011.07.006",
language = "English",
volume = "22",
pages = "393--399",
journal = "Seminars in Cell and Developmental Biology",
issn = "1084-9521",
publisher = "Elsevier",
number = "4",

}

RIS

TY - JOUR

T1 - How synapsin I may cluster synaptic vesicles

AU - Shupliakov, Oleg

AU - Haucke, Volker

AU - Pechstein, Arndt

PY - 2011/1/1

Y1 - 2011/1/1

N2 - Synapsin I is the most abundant brain phosphoprotein present in conventional synapses of the CNS. Knockout and rescue experiments have demonstrated that synapsin is essential for clustering of synaptic vesicles (SVs) at active zones and the organization of the reserve pool of SVs. However, in spite of intense efforts it remains largely unknown how exactly synapsin I performs this function. It has been proposed that synapsin I in its dephosphorylated state may tether SVs to actin filaments within the cluster from where SVs are released in response to activity-induced synapsin phosphorylation. Recent studies, however, have failed to detect actin filaments inside the vesicle cluster at resting central synapses. Instead, proteins with established functional roles in SV recycling have been found within this presynaptic compartment. Here we discuss potential alternative mechanisms of synapsin I-dependent SV clustering in the reserve pool.

AB - Synapsin I is the most abundant brain phosphoprotein present in conventional synapses of the CNS. Knockout and rescue experiments have demonstrated that synapsin is essential for clustering of synaptic vesicles (SVs) at active zones and the organization of the reserve pool of SVs. However, in spite of intense efforts it remains largely unknown how exactly synapsin I performs this function. It has been proposed that synapsin I in its dephosphorylated state may tether SVs to actin filaments within the cluster from where SVs are released in response to activity-induced synapsin phosphorylation. Recent studies, however, have failed to detect actin filaments inside the vesicle cluster at resting central synapses. Instead, proteins with established functional roles in SV recycling have been found within this presynaptic compartment. Here we discuss potential alternative mechanisms of synapsin I-dependent SV clustering in the reserve pool.

KW - Endocytic proteins

KW - Synapse

KW - Synapsin

KW - Synaptic vesicle

KW - Vesicle clustering

UR - http://www.scopus.com/inward/record.url?scp=80052748802&partnerID=8YFLogxK

U2 - 10.1016/j.semcdb.2011.07.006

DO - 10.1016/j.semcdb.2011.07.006

M3 - Review article

AN - SCOPUS:80052748802

VL - 22

SP - 393

EP - 399

JO - Seminars in Cell and Developmental Biology

JF - Seminars in Cell and Developmental Biology

SN - 1084-9521

IS - 4

ER -

ID: 40828994