The syntaxin family of vesicular transport receptors

Mark K. Bennett; JoséE E. Garcia-Arrarás; Lisa A. Elferink; Karen Peterson; Anne M. Fleming; Christopher D. Hazuka; Richard H. Scheller

doi:10.1016/0092-8674(93)90466-4

The syntaxin family of vesicular transport receptors

Mark K. Bennett, JoséE E. Garcia-Arrarás, Lisa A. Elferink, Karen Peterson, Anne M. Fleming, Christopher D. Hazuka, Richard H. Scheller

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

581 Scopus citations

Abstract

Syntaxins A and B are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane. A family of syntaxin-related proteins from rat has been identified that shares 23%-84% amino acid identity. Each of the six syntaxins terminate with a carboxy-terminal hydrophobic domain that anchors the protein on the cytoplasmic surface of cellular membranes. The syntaxins display a broad tissue distribution and, when expressed in COS cells, are targeted to different subcellular compartments. Microinjection studies suggest that the nervous system-specific syntaxin 1A is important for calcium-regulated secretion from neuroendocrine PC12 cells. These results indicate that the syntaxins are a family of receptors for intracellular transport vesicles and that each target membrane may be identified by a specific member of the syntaxin family.

Original language	English (US)
Pages (from-to)	863-873
Number of pages	11
Journal	Cell
Volume	74
Issue number	5
DOIs	https://doi.org/10.1016/0092-8674(93)90466-4
State	Published - Sep 10 1993
Externally published	Yes

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

Access to Document

10.1016/0092-8674(93)90466-4

Cite this

@article{bd379ff4e2d647dc8e7a97ea3a7e6fc1,

title = "The syntaxin family of vesicular transport receptors",

abstract = "Syntaxins A and B are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane. A family of syntaxin-related proteins from rat has been identified that shares 23%-84% amino acid identity. Each of the six syntaxins terminate with a carboxy-terminal hydrophobic domain that anchors the protein on the cytoplasmic surface of cellular membranes. The syntaxins display a broad tissue distribution and, when expressed in COS cells, are targeted to different subcellular compartments. Microinjection studies suggest that the nervous system-specific syntaxin 1A is important for calcium-regulated secretion from neuroendocrine PC12 cells. These results indicate that the syntaxins are a family of receptors for intracellular transport vesicles and that each target membrane may be identified by a specific member of the syntaxin family.",

author = "Bennett, {Mark K.} and Garcia-Arrar{\'a}s, {Jos{\'e}E E.} and Elferink, {Lisa A.} and Karen Peterson and Fleming, {Anne M.} and Hazuka, {Christopher D.} and Scheller, {Richard H.}",

note = "Funding Information: The first three authors (M. K. B., J. E. G.-A., and L. A. E.) have contributed equally to this work. Correspondence should be addressed to R. H. S. We thank Colin Barnstable, Ruth Angeletti, and Suzanne Pfeffer for their kind gifts of antibodies, lain Dawson for providing the Drosophila SED5 DNA, and Sandy Bajjaliah for critical reading of the manuscript. J. E. G.-A. is on sabbatical leave from the University of Puerto Rico and is the recipient of a Minority Access to Research Careers-Nattonal Institute of General Medical Science faculty development fellowship. C. D. t-l. is supported by a National Science Foundation predoctoral fellowship. Financral support was provided by the National Institute of Mental Health.",

year = "1993",

month = sep,

day = "10",

doi = "10.1016/0092-8674(93)90466-4",

language = "English (US)",

volume = "74",

pages = "863--873",

journal = "Cell",

issn = "0092-8674",

publisher = "Cell Press",

number = "5",

}

TY - JOUR

T1 - The syntaxin family of vesicular transport receptors

AU - Bennett, Mark K.

AU - Garcia-Arrarás, JoséE E.

AU - Elferink, Lisa A.

AU - Peterson, Karen

AU - Fleming, Anne M.

AU - Hazuka, Christopher D.

AU - Scheller, Richard H.

N1 - Funding Information: The first three authors (M. K. B., J. E. G.-A., and L. A. E.) have contributed equally to this work. Correspondence should be addressed to R. H. S. We thank Colin Barnstable, Ruth Angeletti, and Suzanne Pfeffer for their kind gifts of antibodies, lain Dawson for providing the Drosophila SED5 DNA, and Sandy Bajjaliah for critical reading of the manuscript. J. E. G.-A. is on sabbatical leave from the University of Puerto Rico and is the recipient of a Minority Access to Research Careers-Nattonal Institute of General Medical Science faculty development fellowship. C. D. t-l. is supported by a National Science Foundation predoctoral fellowship. Financral support was provided by the National Institute of Mental Health.

PY - 1993/9/10

Y1 - 1993/9/10

N2 - Syntaxins A and B are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane. A family of syntaxin-related proteins from rat has been identified that shares 23%-84% amino acid identity. Each of the six syntaxins terminate with a carboxy-terminal hydrophobic domain that anchors the protein on the cytoplasmic surface of cellular membranes. The syntaxins display a broad tissue distribution and, when expressed in COS cells, are targeted to different subcellular compartments. Microinjection studies suggest that the nervous system-specific syntaxin 1A is important for calcium-regulated secretion from neuroendocrine PC12 cells. These results indicate that the syntaxins are a family of receptors for intracellular transport vesicles and that each target membrane may be identified by a specific member of the syntaxin family.

AB - Syntaxins A and B are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane. A family of syntaxin-related proteins from rat has been identified that shares 23%-84% amino acid identity. Each of the six syntaxins terminate with a carboxy-terminal hydrophobic domain that anchors the protein on the cytoplasmic surface of cellular membranes. The syntaxins display a broad tissue distribution and, when expressed in COS cells, are targeted to different subcellular compartments. Microinjection studies suggest that the nervous system-specific syntaxin 1A is important for calcium-regulated secretion from neuroendocrine PC12 cells. These results indicate that the syntaxins are a family of receptors for intracellular transport vesicles and that each target membrane may be identified by a specific member of the syntaxin family.

UR - http://www.scopus.com/inward/record.url?scp=0027328483&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027328483&partnerID=8YFLogxK

U2 - 10.1016/0092-8674(93)90466-4

DO - 10.1016/0092-8674(93)90466-4

M3 - Article

C2 - 7690687

AN - SCOPUS:0027328483

VL - 74

SP - 863

EP - 873

JO - Cell

JF - Cell

SN - 0092-8674

IS - 5

ER -

The syntaxin family of vesicular transport receptors

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this