Clathrin and synaptic vesicle endocytosis: Studies at the squid giant synapse

G. J. Augustine; J. R. Morgan; C. A. Villalba-Galea; S. Jin; K. Prasad; E. M. Lafer

doi:10.1042/BST0340068

Clathrin and synaptic vesicle endocytosis: Studies at the squid giant synapse

G. J. Augustine, J. R. Morgan, C. A. Villalba-Galea, S. Jin, K. Prasad, E. M. Lafer

Biochemistry & Structural Biology

Research output: Contribution to journal › Article › peer-review

29 Scopus citations

Abstract

The role of clathrin-mediated endocytosis in SV (synaptic vesicle) recycling has been studied by combining molecular biology, physiology and electron microscopy at the squid giant synapse. Procedures that prevent clathrin from assembling into membrane coats, such as impairment of binding of the AP180 and AP-2 adaptor proteins, completely prevent membrane budding during endocytosis. These procedures also reduce exocytosis, presumably an indirect effect of a reduction in the number of SVs following block of endocytosis. Disrupting the binding of auxilin to Hsc70 (heat-shock cognate 70) prevents clathrin-coated vesicles from uncoating and also disrupts SV recycling. Taken together, these results indicate that a clathrin-dependent pathway is the primary means of SV recycling at this synapse under physiological conditions.

Original language	English (US)
Pages (from-to)	68-72
Number of pages	5
Journal	Biochemical Society transactions
Volume	34
Issue number	1
DOIs	https://doi.org/10.1042/BST0340068
State	Published - Feb 2006

Keywords

Adaptor protein
Clathrin
Plasma membrane
Squid giant synapse
Synaptic vesicle
Vesicle recycling

ASJC Scopus subject areas

Biochemistry

Access to Document

10.1042/BST0340068

Fingerprint Dive into the research topics of 'Clathrin and synaptic vesicle endocytosis: Studies at the squid giant synapse'. Together they form a unique fingerprint.

Cite this

@article{c9cf8ba8fa61498fa3a494e04958891c,

title = "Clathrin and synaptic vesicle endocytosis: Studies at the squid giant synapse",

abstract = "The role of clathrin-mediated endocytosis in SV (synaptic vesicle) recycling has been studied by combining molecular biology, physiology and electron microscopy at the squid giant synapse. Procedures that prevent clathrin from assembling into membrane coats, such as impairment of binding of the AP180 and AP-2 adaptor proteins, completely prevent membrane budding during endocytosis. These procedures also reduce exocytosis, presumably an indirect effect of a reduction in the number of SVs following block of endocytosis. Disrupting the binding of auxilin to Hsc70 (heat-shock cognate 70) prevents clathrin-coated vesicles from uncoating and also disrupts SV recycling. Taken together, these results indicate that a clathrin-dependent pathway is the primary means of SV recycling at this synapse under physiological conditions.",

keywords = "Adaptor protein, Clathrin, Plasma membrane, Squid giant synapse, Synaptic vesicle, Vesicle recycling",

author = "Augustine, {G. J.} and Morgan, {J. R.} and Villalba-Galea, {C. A.} and S. Jin and K. Prasad and Lafer, {E. M.}",

year = "2006",

month = feb,

doi = "10.1042/BST0340068",

language = "English (US)",

volume = "34",

pages = "68--72",

journal = "Biochemical Society Transactions",

issn = "0300-5127",

publisher = "Portland Press Ltd.",

number = "1",

}

TY - JOUR

T1 - Clathrin and synaptic vesicle endocytosis

T2 - Studies at the squid giant synapse

AU - Augustine, G. J.

AU - Morgan, J. R.

AU - Villalba-Galea, C. A.

AU - Jin, S.

AU - Prasad, K.

AU - Lafer, E. M.

PY - 2006/2

Y1 - 2006/2

N2 - The role of clathrin-mediated endocytosis in SV (synaptic vesicle) recycling has been studied by combining molecular biology, physiology and electron microscopy at the squid giant synapse. Procedures that prevent clathrin from assembling into membrane coats, such as impairment of binding of the AP180 and AP-2 adaptor proteins, completely prevent membrane budding during endocytosis. These procedures also reduce exocytosis, presumably an indirect effect of a reduction in the number of SVs following block of endocytosis. Disrupting the binding of auxilin to Hsc70 (heat-shock cognate 70) prevents clathrin-coated vesicles from uncoating and also disrupts SV recycling. Taken together, these results indicate that a clathrin-dependent pathway is the primary means of SV recycling at this synapse under physiological conditions.

AB - The role of clathrin-mediated endocytosis in SV (synaptic vesicle) recycling has been studied by combining molecular biology, physiology and electron microscopy at the squid giant synapse. Procedures that prevent clathrin from assembling into membrane coats, such as impairment of binding of the AP180 and AP-2 adaptor proteins, completely prevent membrane budding during endocytosis. These procedures also reduce exocytosis, presumably an indirect effect of a reduction in the number of SVs following block of endocytosis. Disrupting the binding of auxilin to Hsc70 (heat-shock cognate 70) prevents clathrin-coated vesicles from uncoating and also disrupts SV recycling. Taken together, these results indicate that a clathrin-dependent pathway is the primary means of SV recycling at this synapse under physiological conditions.

KW - Adaptor protein

KW - Clathrin

KW - Plasma membrane

KW - Squid giant synapse

KW - Synaptic vesicle

KW - Vesicle recycling

UR - http://www.scopus.com/inward/record.url?scp=32544434839&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=32544434839&partnerID=8YFLogxK

U2 - 10.1042/BST0340068

DO - 10.1042/BST0340068

M3 - Article

C2 - 16417485

AN - SCOPUS:32544434839

VL - 34

SP - 68

EP - 72

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

SN - 0300-5127

IS - 1

ER -