A targeting signal in VAMP regulating transport to synaptic vesicles

Eric Grote; Joe C. Hao; Mark K. Bennett; Regis B. Kelly

doi:10.1016/0092-8674(95)90079-9

A targeting signal in VAMP regulating transport to synaptic vesicles

Eric Grote, Joe C. Hao, Mark K. Bennett, Regis B. Kelly

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

143 Scopus citations

Abstract

VAMP is a synaptic vesicle membrane protein required for fusion. Synaptic vesicle targeting was measured for mutants of an epitope-tagged form of VAMP in transfected PC12 cells. A signal within a predicted amphipathic α helix is essential for targeting to synaptic vesicles. Cellubrevin, a nonneural VAMP homolog, contains this signal and is also targeted to synaptic vesicles. Amino acid substitutions within the synaptic vesicle targeting signal either enhance or inhibit sorting of VAMP to synaptic vesicles, but do not affect the ability of VAMP to form complexes with syntaxin and SNAP-25.

Original language	English (US)
Pages (from-to)	581-589
Number of pages	9
Journal	Cell
Volume	81
Issue number	4
DOIs	https://doi.org/10.1016/0092-8674(95)90079-9
State	Published - May 19 1995
Externally published	Yes

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

Access to Document

10.1016/0092-8674(95)90079-9

Cite this

@article{d3940cd14dcb47c0b0a003c260e3d31b,

title = "A targeting signal in VAMP regulating transport to synaptic vesicles",

abstract = "VAMP is a synaptic vesicle membrane protein required for fusion. Synaptic vesicle targeting was measured for mutants of an epitope-tagged form of VAMP in transfected PC12 cells. A signal within a predicted amphipathic α helix is essential for targeting to synaptic vesicles. Cellubrevin, a nonneural VAMP homolog, contains this signal and is also targeted to synaptic vesicles. Amino acid substitutions within the synaptic vesicle targeting signal either enhance or inhibit sorting of VAMP to synaptic vesicles, but do not affect the ability of VAMP to form complexes with syntaxin and SNAP-25.",

author = "Eric Grote and Hao, {Joe C.} and Bennett, {Mark K.} and Kelly, {Regis B.}",

note = "Funding Information: We thank members of the Kelly laboratory for valuable discussions throughout the course of this work. The VAMP-2 cDNA expression vector was a generous gift of Richard Scheller. Antibodies used in this study were provided by Reinhard Jahn, Thomas Siidhof, and William Trimble. This work was supported by National Institutes of Health grants DK09878 and DK33937 to R. B. K. and GM51313 to M. K. 8.",

year = "1995",

month = may,

day = "19",

doi = "10.1016/0092-8674(95)90079-9",

language = "English (US)",

volume = "81",

pages = "581--589",

journal = "Cell",

issn = "0092-8674",

publisher = "Cell Press",

number = "4",

}

TY - JOUR

T1 - A targeting signal in VAMP regulating transport to synaptic vesicles

AU - Grote, Eric

AU - Hao, Joe C.

AU - Bennett, Mark K.

AU - Kelly, Regis B.

N1 - Funding Information: We thank members of the Kelly laboratory for valuable discussions throughout the course of this work. The VAMP-2 cDNA expression vector was a generous gift of Richard Scheller. Antibodies used in this study were provided by Reinhard Jahn, Thomas Siidhof, and William Trimble. This work was supported by National Institutes of Health grants DK09878 and DK33937 to R. B. K. and GM51313 to M. K. 8.

PY - 1995/5/19

Y1 - 1995/5/19

N2 - VAMP is a synaptic vesicle membrane protein required for fusion. Synaptic vesicle targeting was measured for mutants of an epitope-tagged form of VAMP in transfected PC12 cells. A signal within a predicted amphipathic α helix is essential for targeting to synaptic vesicles. Cellubrevin, a nonneural VAMP homolog, contains this signal and is also targeted to synaptic vesicles. Amino acid substitutions within the synaptic vesicle targeting signal either enhance or inhibit sorting of VAMP to synaptic vesicles, but do not affect the ability of VAMP to form complexes with syntaxin and SNAP-25.

AB - VAMP is a synaptic vesicle membrane protein required for fusion. Synaptic vesicle targeting was measured for mutants of an epitope-tagged form of VAMP in transfected PC12 cells. A signal within a predicted amphipathic α helix is essential for targeting to synaptic vesicles. Cellubrevin, a nonneural VAMP homolog, contains this signal and is also targeted to synaptic vesicles. Amino acid substitutions within the synaptic vesicle targeting signal either enhance or inhibit sorting of VAMP to synaptic vesicles, but do not affect the ability of VAMP to form complexes with syntaxin and SNAP-25.

UR - http://www.scopus.com/inward/record.url?scp=0029005106&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029005106&partnerID=8YFLogxK

U2 - 10.1016/0092-8674(95)90079-9

DO - 10.1016/0092-8674(95)90079-9

M3 - Article

C2 - 7758112

AN - SCOPUS:0029005106

SN - 0092-8674

VL - 81

SP - 581

EP - 589

JO - Cell

JF - Cell

IS - 4

ER -

A targeting signal in VAMP regulating transport to synaptic vesicles

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this