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Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes.

Prekeris R, Klumperman J, Chen YA, Scheller RH - J. Cell Biol. (1998)

Bottom Line: Additional labeling is also present in endosomal vacuoles, where it is often found in clathrin-coated membrane areas.This complex(es) binds exogenously added alphaSNAP and NSF and dissociates in the presence of ATP, but not ATPgammaS.These results support a role for syntaxin 13 in membrane fusion events during the recycling of plasma membrane proteins.

View Article: PubMed Central - PubMed

Affiliation: Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California 94305-5428, USA.

ABSTRACT
Endocytosis-mediated recycling of plasma membrane is a critical vesicle trafficking step important in diverse biological processes. The membrane trafficking decisions and sorting events take place in a series of heterogeneous and highly dynamic organelles, the endosomes. Syntaxin 13, a recently discovered member of the syntaxin family, has been suggested to play a role in mediating endosomal trafficking. To better understand the function of syntaxin 13 we examined its intracellular distribution in nonpolarized cells. By confocal immunofluorescence and electron microscopy, syntaxin 13 is primarily found in tubular early and recycling endosomes, where it colocalizes with transferrin receptor. Additional labeling is also present in endosomal vacuoles, where it is often found in clathrin-coated membrane areas. Furthermore, anti-syntaxin 13 antibody inhibits transferrin receptor recycling in permeabilized PC12 cells. Immunoprecipitation of syntaxin 13 revealed that, in Triton X-100 extracts, syntaxin 13 is present in a complex(es) comprised of betaSNAP, VAMP 2/3, and SNAP-25. This complex(es) binds exogenously added alphaSNAP and NSF and dissociates in the presence of ATP, but not ATPgammaS. These results support a role for syntaxin 13 in membrane fusion events during the recycling of plasma membrane proteins.

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Related in: MedlinePlus

Double-immunogold labeling of syntaxin 13 and TfR (gold sizes are indicated on the pictures) showing extensive colocalization (small arrowheads) in the tubulovesicular membrane clusters. (B) Large arrowhead, a syntaxin 13/TfR-positive tubule connected  with early endosome (EE) vacuole. G, Golgi complex; N, nucleus; P, plasma membrane. Bar, 200 nm.
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Figure 7: Double-immunogold labeling of syntaxin 13 and TfR (gold sizes are indicated on the pictures) showing extensive colocalization (small arrowheads) in the tubulovesicular membrane clusters. (B) Large arrowhead, a syntaxin 13/TfR-positive tubule connected with early endosome (EE) vacuole. G, Golgi complex; N, nucleus; P, plasma membrane. Bar, 200 nm.

Mentions: Double-immunogold labeling of syntaxin 13 and TfR revealed a high degree of colocalization in the tubulovesicular membrane profiles, both near endosomal vacuoles and Golgi complexes (Fig. 7). Of all individual vesicles and larger tubules that were positive for syntaxin 13, ∼50% were labeled for TfR as well. Finally, this double labeling revealed that syntaxin 13 was mainly present on the tubulovesicular network of EE and RE that harbored TfR as well.


Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes.

Prekeris R, Klumperman J, Chen YA, Scheller RH - J. Cell Biol. (1998)

Double-immunogold labeling of syntaxin 13 and TfR (gold sizes are indicated on the pictures) showing extensive colocalization (small arrowheads) in the tubulovesicular membrane clusters. (B) Large arrowhead, a syntaxin 13/TfR-positive tubule connected  with early endosome (EE) vacuole. G, Golgi complex; N, nucleus; P, plasma membrane. Bar, 200 nm.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2132958&req=5

Figure 7: Double-immunogold labeling of syntaxin 13 and TfR (gold sizes are indicated on the pictures) showing extensive colocalization (small arrowheads) in the tubulovesicular membrane clusters. (B) Large arrowhead, a syntaxin 13/TfR-positive tubule connected with early endosome (EE) vacuole. G, Golgi complex; N, nucleus; P, plasma membrane. Bar, 200 nm.
Mentions: Double-immunogold labeling of syntaxin 13 and TfR revealed a high degree of colocalization in the tubulovesicular membrane profiles, both near endosomal vacuoles and Golgi complexes (Fig. 7). Of all individual vesicles and larger tubules that were positive for syntaxin 13, ∼50% were labeled for TfR as well. Finally, this double labeling revealed that syntaxin 13 was mainly present on the tubulovesicular network of EE and RE that harbored TfR as well.

Bottom Line: Additional labeling is also present in endosomal vacuoles, where it is often found in clathrin-coated membrane areas.This complex(es) binds exogenously added alphaSNAP and NSF and dissociates in the presence of ATP, but not ATPgammaS.These results support a role for syntaxin 13 in membrane fusion events during the recycling of plasma membrane proteins.

View Article: PubMed Central - PubMed

Affiliation: Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California 94305-5428, USA.

ABSTRACT
Endocytosis-mediated recycling of plasma membrane is a critical vesicle trafficking step important in diverse biological processes. The membrane trafficking decisions and sorting events take place in a series of heterogeneous and highly dynamic organelles, the endosomes. Syntaxin 13, a recently discovered member of the syntaxin family, has been suggested to play a role in mediating endosomal trafficking. To better understand the function of syntaxin 13 we examined its intracellular distribution in nonpolarized cells. By confocal immunofluorescence and electron microscopy, syntaxin 13 is primarily found in tubular early and recycling endosomes, where it colocalizes with transferrin receptor. Additional labeling is also present in endosomal vacuoles, where it is often found in clathrin-coated membrane areas. Furthermore, anti-syntaxin 13 antibody inhibits transferrin receptor recycling in permeabilized PC12 cells. Immunoprecipitation of syntaxin 13 revealed that, in Triton X-100 extracts, syntaxin 13 is present in a complex(es) comprised of betaSNAP, VAMP 2/3, and SNAP-25. This complex(es) binds exogenously added alphaSNAP and NSF and dissociates in the presence of ATP, but not ATPgammaS. These results support a role for syntaxin 13 in membrane fusion events during the recycling of plasma membrane proteins.

Show MeSH
Related in: MedlinePlus