Targeting vesicles to specific sites on the plasma membrane: the role of the sec6/8 complex

The delivery of secretory vesicles to appropriate docking and fusion sites on the plasma membrane is crucial for many cellular functions, including formation of synapses, exocytosis of neurotransmitter, establishment and maintenance of cell polarity, cell growth and plasma membrane wound healing. Ce...

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Published inTrends in Cell Biology Vol. 9; no. 4; pp. 150 - 153
Main Authors Hsu, Shu-Chan, Hazuka, Christopher D, Foletti, Davide L, Scheller, Richard H
Format Book Review Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.04.1999
Subjects
Animals
Carrier Proteins - physiology
Cell Line
Cell Membrane - metabolism
Cytoplasmic Granules - secretion
Dogs
Evolution, Molecular
Exocytosis - physiology
Fungal Proteins - physiology
Genes, Lethal
Macromolecular Substances
Mammals - metabolism
Mice
Models, Biological
Nerve Tissue Proteins - physiology
Organelles - metabolism
plasma membrane
protein secretion
Rats
Saccharomyces cerevisiae - physiology
Saccharomyces cerevisiae Proteins
sec6 protein
sec8 protein
secretion
secretory pathway
Signal Transduction
Species Specificity
vesicle docking
vesicle transport
vesicular traffic
Vesicular Transport Proteins
Neuroscience
secretion
plasma membrane
Cell biology
secretory pathway
Biochemistry
vesicle docking
vesicle transport
protein secretion
vesicular traffic
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Abstract The delivery of secretory vesicles to appropriate docking and fusion sites on the plasma membrane is crucial for many cellular functions, including formation of synapses, exocytosis of neurotransmitter, establishment and maintenance of cell polarity, cell growth and plasma membrane wound healing. Cell-biological, genetic and biochemical approaches have identified crucial proteins and protein interactions important for vesicle docking and fusion. However, a description of the molecular mechanisms underlying vesicle targeting to specific membrane-fusion sites remains elusive. This review discusses a set of proteins that might direct vesicles to specific domains of the plasma membrane.
AbstractList The delivery of secretory vesicles to appropriate docking and fusion sites on the plasma membrane is crucial for many cellular functions, including formation of synapses, exocytosis of neurotransmitter, establishment and maintenance of cell polarity, cell growth and plasma membrane wound healing. Cell-biological, genetic and biochemical approaches have identified crucial proteins and protein interactions important for vesicle docking and fusion. However, a description of the molecular mechanisms underlying vesicle targeting to specific membrane-fusion sites remains elusive. This review discusses a set of proteins that might direct vesicles to specific domains of the plasma membrane.
Author Hsu, Shu-Chan
Foletti, Davide L
Hazuka, Christopher D
Scheller, Richard H
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  surname: Scheller
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  email: scheller@cmgm.stanford.edu
BackLink https://www.ncbi.nlm.nih.gov/pubmed/10203793$$D View this record in MEDLINE/PubMed
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Keywords Neuroscience
secretion
plasma membrane
Cell biology
secretory pathway
Biochemistry
vesicle docking
vesicle transport
protein secretion
vesicular traffic
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Snippet The delivery of secretory vesicles to appropriate docking and fusion sites on the plasma membrane is crucial for many cellular functions, including formation...
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SubjectTerms Animals
Carrier Proteins - physiology
Cell Line
Cell Membrane - metabolism
Cytoplasmic Granules - secretion
Dogs
Evolution, Molecular
Exocytosis - physiology
Fungal Proteins - physiology
Genes, Lethal
Macromolecular Substances
Mammals - metabolism
Mice
Models, Biological
Nerve Tissue Proteins - physiology
Organelles - metabolism
plasma membrane
protein secretion
Rats
Saccharomyces cerevisiae - physiology
Saccharomyces cerevisiae Proteins
sec6 protein
sec8 protein
secretion
secretory pathway
Signal Transduction
Species Specificity
vesicle docking
vesicle transport
vesicular traffic
Vesicular Transport Proteins
Title Targeting vesicles to specific sites on the plasma membrane: the role of the sec6/8 complex
URI https://dx.doi.org/10.1016/S0962-8924(99)01516-0
https://www.ncbi.nlm.nih.gov/pubmed/10203793
https://search.proquest.com/docview/17485556
https://search.proquest.com/docview/69695951
Volume 9
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